How SH3 domains recognize proline

Advances in Protein Chemistry

Volumn 61, Issue , 2002, Pages 211-268

  Musacchio, Andrea ^a  

^a EUROPEAN INSTITUTE OF ONCOLOGY   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

POLYPROLINE; PROLINE; PROTEIN; UNCLASSIFIED DRUG;

BINDING AFFINITY; BINDING SITE; CONSENSUS SEQUENCE; LIGAND BINDING; MACROMOLECULE; MOLECULAR INTERACTION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; REVIEW; SRC HOMOLOGY DOMAIN;

EID: 0036420970     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(02)61006-X     Document Type: Review

References (236)

1. Kay, B. K., Williamson, M. P., and Sudol, M. (2000). The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231-241.
2. Sudol, M. (1998). From Src homology domains to other signaling modules: Proposal of the 'protein recognition code.' Oncogene 17, 1469-1474.
3. MacArthur, M. W., and Thornton, J. M. (1991). Influence of proline residues on protein conformation. J. Mol. Biol. 218, 397-412.
4. Williamson, M. P. (1994). The structure and function of proline-rich regions in proteins. Biochem. J. 297, 249-260.
5. Siligardi, G., and Drake, A. F. (1995). The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides. Biopolymers 37, 281-292.
6. Cowan, P. M., and McGavin, S. (1955). Structure of poly-L-proline. Nature 176, 470-478.
7. Stapley, B. J., and Creamer, T. F. (1995). A survey of left-handed polyproline II helices. Protein Sci. 8, 587-595.
8. Adzhubei, A. A., and Sternberg, M. J. (1993). Left-handed polyproline II helices commonly occur in globular proteins. J. Mol. Biol. 229, 472-493.
9. Sreerama, N., and Woody, R. W. (1994). Poly(pro)II helices in globular proteins: Identification and circular dichroic analysis. Biochemistry 33, 10022-10025.
10. Adzhubei, A. A., and Sternberg, M. J. (1994). Conservation of polyproline II helices in homologous proteins: Implications for structure prediction by model building. Protein Sci. 3, 2395-2410.
11. Chang, A., Cheang, S., Espanel, X., and Sudol, M. (2000). Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 275, 20562-20571.
12. Bienkiewicz, E. A., Moon Woody, A., and Woody, R. W. (2000). Conformation of the RNA polymerase II C-terminal domain: Circular dichroism of long and short fragments. J. Mol. Biol. 297, 119-133.
13. Bousquet, J. A., Garbay, C., Roques, B. P., and Mely, Y. (2000). Circular dichroic investigation of the native and non-native conformational states of the growth factor receptor-binding protein 2 N-terminal src homology domain 3: Effect of binding to a proline-rich peptide from guanine nucleotide exchange factor. Biochemistry 39, 7722-7735.
14. Viguera, A. R., Arrondo, J. L., Musacchio, A., Saraste, M., and Serrano, L. (1994). Characterization of the interaction of natural proline-rich peptides with five different SH3 domains. Biochemistry 33, 10925-10933.
15. Renzoni, D. A., Pugh, D. J., Siligardi, G., Das, P., Morton, C. J., Rossi, C., Waterfield, M. D., Campbell, I. D., and Ladbury, J. E. (1996). Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of P13-kinase. Biochemistry 35, 15646-15653.
16. Morton, C. J., Pugh, D. J., Brown, E. L., Kahmann, J. D., Renzoni, D. A., and Campbell, I. D. (1996). Solution structure and peptide binding of the SH3 domain from human Fyn. Structure 4, 705-714.
17. Dong, J., Misselwitz, R., Welfle, H., and Westermann, P. (2000). Expression and purification of dynamin II domains and initial studies on structure and function. Protein Expr. Purif. 20, 314-323.
18. Jardetzky, T. S., Brown, J. H., Gorga, J. C., Stern, L. J., Urban, R. G., Strominger, J. L., and Wiley, D. C. (1996). Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. Proc. Natl. Acad. Sci. USA 93, 734-738.
19. Stern, L. J., Brown, J. H., Jardetzky, T. S., Gorga, J. C., Urban, R. G., Strominger, J. L., and Wiley, D. C. (1994). Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368, 215-221.
20. Sicheri, F., Moarefi, I., and Kuriyan, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609.
21. Xu, W., Harrison, S. C., and Eck, M. J. (1997). Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602.
22. Williams, J. C., Weijland, A., Gonfloni, S., Thompson, A., Courtneidge, S. A., Superti-Furga, G., and Wierenga, R. K. (1997). The 2.35 Å crystal structure of the inactivated form of chicken Src: A dynamic molecule with multiple regulatory interactions. J. Mol. Biol. 274, 757-775.
23. Creamer, T. P. (1998). Left-handed polyproline II helix formation is (very) locally driven. Proteins 33, 218-226.
24. Mayer, B. J. (2001). SH3 domains: Complexity in moderation. J. Cell Sci. 114, 1253-1263.
25. Schlessinger, J. (1994). SH2/SH3 signaling proteins. Curr. Opin. Genet. Dev. 4, 25-30.
26. Cohen, G. B., Ren, R., and Baltimore, D. (1995). Modular binding domains in signal transduction proteins. Cell 80, 237-248.
27. Kay, B. K., Williamson, M. P., and Sudol, M. (2000). The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231-241.
28. Pawson, T., and Nash, P. (2000). Protein-protein interactions define specificity in signal transduction. Genes Dev. 14, 1027-1047.
29. Schultz, J., Copley, R. R., Doerks, T., Ponting, C. P., and Bork, P. (2000). SMART: A Web-based tool for the study of genetically mobile domains. Nucleic Acids Res. 28, 231-234.
30. Schlessinger, J. (1993). How receptor tyrosine kinases activate Ras. Trends Biochem Sci. 18, 273-275.
31. Yu, H., Rosen, M. K., Shin, T. B., Seidel-Dugan, C., Brugge, J. S., and Schreiber, S. L. (1992). Solution structure of the SH3 domain of Src and identification of its ligand-binding site. Science 258, 1665-1668.
32. Musacchio, A., Noble, M., Pauptit, R., Wierenga, R., and Saraste, M. (1992). Crystal structure of a Src-homology 3 (SH3) domain. Nature 359, 851-855.
33. Kohda, D., Hatanaka, H., Odaka, M., Mandiyan, V., Ullrich, A., Schlessinger, J., and Inagaki, F. (1993). Solution structure of the SH3 domain of phospholipase C-gamma. Cell 72, 953-960.
34. Koyama, S., Yu, H., Dalgarno, D. C., Shin, T. B., Zydowsky, L. D., and Schreiber, S. L. (1993). Structure of the PI3K SH3 domain and analysis of the SH3 family. Cell 72, 945-952.
35. Booker, G. W., Gout, I., Downing, A. K., Driscoll, P. C., Boyd, J., Waterfield, M. D., and Campbell, I. D. (1993). Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase. Cell 73, 813-822.
36. Noble, M. E., Musacchio, A., Saraste, M., Courtneidge, S. A., and Wierenga, R. K. (1993). Crystal structure of the SH3 domain in human Fyn: Comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin. EMBO J. 12, 2617-2624.
37. Musacchio, A., Wilmanns, M., and Saraste, M. (1994). Structure and function of the SH3 domain. Prog. Biophys. Mol. Biol. 61, 283-297.
38. Whisstock, J. C., and Lesk, A. M. (1999). SH3 domains in prokaryotes. Trends Biochem. Sci. 24, 132-133.
39. Kortemme, T., Kelly, M. J., Kay, L. E., Forman-Kay, J., and Serrano, L. (2000). Similarities between the spectrin SH3 domain denatured state and its folding transition state. J. Mol. Biol. 297, 1217-1229.
40. Li, L., Mirny, L. A., and Shakhnovich, E. I. (2000). Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus. Nat. Struct. Biol. 7, 336-342.
41. Fersht, A. R. (2000). Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism. Proc. Natl. Acad. Sci. USA 97, 1525-1529.
42. Gu, H., Doshi, N., Kim, D. E., Simons, K. T., Santiago, J. V., Nauli, S., and Baker, D. (1999). Robustness of protein folding kinetics to surface hydrophobic substitutions. Protein Sci. 8, 2734-2741.
43. Riddle, D. S., Grantcharova, V. P., Santiago, J. V., Alm, E., Ruczinski, I., and Baker, D. (1999). Experiment and theory highlight role of native state topology in SH3 folding. Nat. Struct. Biol. 6, 1016-1024.
44. Martinez, J. C., and Serrano, L. (1999). The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat. Struct. Biol. 6, 1010-1016.
45. Tsai, J., Levitt, M., and Baker, D. (1999). Hierarchy of structure loss in MD simulations of src SH3 domain unfolding. J. Mol. Biol. 291, 215-225.
46. Sadqi, M., Casares, S., Abril, M. A., Lopez-Mayorga, O., Conejero-Lara, F., and Freire, E. (1999). The native state conformational ensemble of the SH3 domain from alphaspectrin. Biochemistry 38, 8899-8906.
47. Larson, S. M., and Davidson, A. R. (2000). The identification of conserved interactions within the SH3 domain by alignment of sequences and structures. Protein Sci. 9, 2170-2180.
48. Guijarro, J. I., Sunde, M., Jones, J. A., Campbell, I. D., and Dobson, C. M. (1998). Amyloid fibril formation by an SH3 domain. Proc. Natl. Acad. Sci. USA 95, 4224-4228.
49. Jimenez, J. L., Guijarro, J. I., Orlova, E., Zurdo, J., Dobson, C. M., Sunde, M., and Saibil, H. R. (1999). Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18, 815-821.
50. Sunde, M., and Blake, C. C. (1998). From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation. Q. Rev. Biophys. 31, 1-39.
51. Kishan, K. V., Scita, G., Wong, W. T., Di Fiore, P. P., and Newcomer, M. E. (1997). The SH3 domain of Eps8 exists as a novel intertwined dimer. Nat. Struct. Biol. 4, 739-743.
52. Mongiovi, A. M., Romano, P. R., Panni, S., Mendoza, M., Wong, W. T., Musacchio, A., Cesareni, G., and Di Fiore, P. P. (1999). A novel peptide-SH3 interaction. EMBO J. 18, 5300-5309.
53. Kishan, K. V., Newcomer, M. E., Rhodes, T. H., and Guilliot, S. D. (2001). Effect of pH and salt bridges on structural assembly: Molecular structures of the monomer and intertwined dimer of the Eps8 SH3 domain. Protein Sci. 10, 1046-1055.
54. Ren, R., Mayer, B. J., Cicchetti, P., and Baltimore, D. (1993). Identification of a tenamino acid proline-rich SH3 binding site. Science 259, 1157-1161.
55. Cicchetti, P., Mayer, B. J., Thiel, G., and Baltimore, D. (1992). Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho. Science 257, 803-806.
56. Cestra, G., Castagnoli, L., Dente, L., Minenkova, O., Petrelli, A., Migone, N., Hoffmuller, U., Schneidèr-Mergener, J., and Cesareni, G. (1999). The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity. J. Biol. Chem. 274, 32001-32007.
57. Kurakin, A., Hoffman, N. G., and Kay, B. K. (1998). Molecular recognition properties of the C-terminal Sh3 domain of the Cbl associated protein, Cap. J. Peptide. Res. 52, 331-337.
58. Sparks, A. B., Rider, J. E., and Kay, B. K. (1998). Mapping the specificity of SH3 domains with phage-displayed random-peptide libraries. Methods Mol. Biol. 84, 87-103.
59. Grabs, D., Slepnev, V. I., Songyang, Z., David, C., Lynch, M., Cantley, L. C., and De Camilli, P. (1997). The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence. J. Biol. Chem. 272, 13419-13425.
60. Yamabhai, M., and Kay, B. K. (1997). Examining the specificity of Src homology 3 domain-ligand interactions with alkaline phosphatase fusion proteins. Anal. Biochem. 247, 143-151.
61. Hoffman, N. G., Sparks, A. B., Carter, J. M., and Kay, B. K. (1996). Binding properties of SH3 peptide ligands identified from phage-displayed random peptide libraries. Mol. Divers. 2, 5-12.
62. Schmitz, R., Baumann, G., and Gram, H. (1996). Catalytic specificity of phosphotyrosine kinases Blk, Lyn, c-Src and Syk as assessed by phage display. J. Mol. Biol. 260, 664-677.
63. Sparks, A. B., Rider, J. E., Hoffman, N. G., Fowlkes, D. M., Quillam, L. A., and Kay, B. K. (1996). Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2. Proc. Natl. Acad. Sci. USA 93, 1540-1544.
64. Sparks, A. B., Quilliam, L. A., Thorn, J. M., Der, C. J., and Kay, B. K. (1994). Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries. J. Biol. Chem. 269, 23853-23856.
65. Yu, H., Chen, J. K., Feng, S., Dalgarno, D. C., Brauer, A. W., and Schreiber, S. L. (1994). Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 76, 933-945.
66. De Leo, F. R., Ulman, K. V., Davis, A. R., Jutila, K. L., and Quinn, M. T. (1996). Assembly of the human neutrophil NADPH oxidase involves binding of p67phox and flavocytochrome b to a common functional domain in p47phox. J. Biol. Chem. 271, 17013-17020.
67. Rickles, R. J., Botfield, M. C., Zhou, X. M., Henry, P. A., Brugge, J. S., and Zoller, M. J. (1995). Phage display selection of ligand residues important for Src homology 3 domain binding specificity. Proc. Natl. Acad. Sci. USA 92, 10909-10913.
68. Rickles, R. J., Botfield, M. C., Weng, Z., Taylor, J. A., Green, O. M., Brugge, J. S., and Zoller, M. J. (1994). Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries. EMBO J. 13, 5598-5604.
69. Cheadle, C., Ivashchenko, Y., South, V., Searfoss, G. H., French, S., Howk, R., Ricca, G. A., and Jaye, M. (1994). Identification of a Src SH3 domain binding motif by screening a random phage display library. J. Biol. Chem. 269, 24034-24039.
70. Simon, J. A., and Schreiber, S. L. (1995). Grb2 SH3 binding to peptides from Sos: Evaluation of a general model for SH3-ligand interactions. Chem. Biol. 2, 53-60.
71. Feng, S., Kapoor, T. M., Shirai, F., Combs, A. P., and Schreiber, S. L. (1996). Molecular basis for the binding of SH3 ligands with non-peptide elements identified by combinatorial synthesis. Chem. Biol. 3, 661-670.
72. Egan, S. E., Giddings, B. W., Brooks, M. W., Buday, L., Sizeland, A. M., and Weinberg, R. A. (1993). Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature 363, 45-51.
73. Rozakis-Adcock, M., Fernley, R., Wade, J., Pawson, T., and Bowtell, D. (1993). The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature 363, 83-85.
74. Buday, L., and Downward, J. (1993). Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor. Cell 73, 611-620.
75. Skolnik, E. Y., Batzer, A., Li, N., Lee, C. H., Lowenstein, E., Mohammadi, M., Margolis, B., and Schlessinger, J. (1993). The function of GRB2 in linking the insulin receptor to Ras signaling pathways. Science 260, 1953-1955.
76. Baltensperger, K., Kozma, L. M., Cherniack, A. D., Klarlund, J. K., Chawla, A., Banerjee, U., and Czech, M. P. (1993). Binding of the Ras activator son of sevenless to insulin receptor substrate-1 signaling complexes. Science 260, 1950-1952.
77. Chardin, P., Camonis, J. H., Gale, N. W., van Aelst, L., Schlessinger, J., Wigler, M. H., and Bar-Sagi, D. (1993). Human Sos1: A guanine nucleotide exchange factor for Ras that binds to GRB2. Science 260, 1338-1343.
78. Li, N., Batzer, A., Daly, R., Yajnik, V., Skolnik, E., Chardin, P., Bar-Sagi, D., Margolis, B., and Schlessinger, J. (1993). Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature 363, 85-88.
79. Gale, N. W., Kaplan, S., Lowenstein, E. J., Schlessinger, J., and Bar-Sagi, D. (1993). Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras. Nature 363, 88-92.
80. Olivier, J. P., Raabe, T., Henkemeyer, M., Dickson, B., Mbamalu, G., Margolis, B., Schlessinger, J., Hafen, E., and Pawson, T. (1993). A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos. Cell 73, 179-191.
81. Brannetti, B., Via, A., Cestra, G., Cesareni, G., and Citterich, M. H. (2000). SH3-SPOT: An algorithm to predict preferred ligands to different members of the SH3 gene family. J. Mol. Biol. 298, 313-328.
82. Yaffe, M. B., Leparc, G. G., Lai, J., Obata, T., Volinia, S., and Cantley, L. C. (2001). A motif-based profile scanning approach for genome-wide prediction of signaling pathways. Nat. Biotechnol. 19, 348-353.
83. Zucconi, A., Dente, L., Santonico, E., Castagnoli, L., and Cesareni, G. (2001). Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1. J. Mol. Biol. 307, 1329-1339.
84. Feng, S., Chen, J. K., Yu, H., Simon, J. A., and Schreiber, S. L. (1994). Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions. Science 266, 1241-1247.
85. Lim, W. A., Richards, F. M., and Fox, R. O. (1994). Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372, 375-379.
86. Musacchio, A., Saraste, M., and Wilmanns, M. (1994). High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat. Struct. Biol. 1, 546-551.
87. Pisabarro, M. T., and Serrano, L. (1996). Rational design of specific high-affinity peptide ligands for the Abl-SH3 domain. Biochemistry 35, 10634-10640.
88. Vidal, M., Goudreau, N., Cornille, F., Cussac, D., Gincel, E., and Garbay, C. (1999). Molecular and cellular analysis of Grb2 SH3 domain mutants: Interaction with Sos and dynamin. J. Mol. Biol. 290, 717-730.
89. Chen, Y. J., Lin, S. C., Tzeng, S. R., Patel, H. V., Lyu, P. C., and Cheng, J. W. (1996). Stability and folding of the SH3 domain of Bruton's tyrosine kinase. Proteins 26, 465-471.
90. Nguyen, J. T., Turck, C. W., Cohen, F. E., Zuckermann, R. N., and Lim, W. A. (1998). Exploiting the basis of proline recognition by SH3 and WW domains: Design of N-substituted inhibitors. Science 282, 2088-2092.
91. Aghazadeh, B., and Rosen, M. K. (1999). Ligand recognition by SH3 and WW domains: The role of N-alkylation in PPII helices. Chem. Biol. 6, R241-R246.
92. Kolafa, J., Perram, J. W., and Bywater, R. P. (2000). Essential motions and energetic contributions of individual residues in a peptide bound to an SH3 domain. Biophys. J. 79, 646-655.
93. Nguyen, J. T., Porter, M., Amoui, M., Miller, W. T., Zuckermann, R. N., and Lim, W. A. (2000). Improving SH3 domain ligand selectivity using a non-natural scaffold. Chem. Biol. 7, 463-473.
94. Fedorov, A. A., Fedorov, E., Gertler, F., and Almo, S. C. (1999). Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function. Nat. Struct. Biol. 6, 661-665.
95. Macias, M. J., Hyvonen, M., Baraldi, E., Schultz, J., Sudol, M., Saraste, M., and Oschkinat, H. (1996). Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature 382, 646-649.
96. Mahoney, N. M., Rozwarski, D. A., Fedorov, E., Fedorov, A. A., and Almo, S. C. (1999). Profilin binds proline-rich ligands in two distinct amide backbone orientations. Nat. Struct. Biol. 6, 666-671.
97. Huang, X., Poy, F., Zhang, R., Joachimiak, A., Sudol, M., and Eck, M. J. (2000). Structure of a WW domain containing fragment of dystrophin in complex with betadystroglycan. Nat. Struct. Biol. 7, 634-638.
98. Wu, X., Knudsen, B., Feller, S. M., Zheng, J., Sali, A., Cowburn, D., Hanafusa, H., and Kuriyan, J. (1995). Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure 3, 215-226.
99. Owen, D. J., Wigge, P., Vallis, Y., Moore, J. D., Evans, P. R., and McMahon, H. T. (1998). Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation. EMBO J. 17, 5273-5285.
100. Feng, S., Kasahara, C., Rickles, R. J., and Schreiber, S. L. (1995). Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands. Proc. Natl. Acad. Sci. USA 92, 12408-12415.
101. Lee, C. H., Saksela, K., Mirza, U. A., Chait, B. T. and Kuriyan, J. (1996). Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85, 931-942.
102. Gorina, S., and Pavletich, N. P. (1996). Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 274, 1001-1005.
103. Ma, Y. C., and Huang, X. Y. (1998). Identification of the binding site for Gqalpha on its effector Bruton's tyrosine kinase. Proc. Natl. Acad. Sci. USA 95, 12197-12201.
104. Sparks, A. B., Hoffman, N. G., McConnell, S. J., Fowlkes, D. M., and Kay, B. K. (1996). Cloning of ligand targets: Systematic isolation of SH3 domain-containing proteins. Nat. Biotechnol. 14, 741-744.
105. Van Etten, R. A. (1999). Cycling, stressed-out and nervous: Cellular functions of c-Abl. Trends Cell Biol. 9, 179-186.
106. Pisabarro, M. T., Serrano, L., and Wilmanns, M. (1998). Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: Implications for SH3-ligand interactions. J. Mol. Biol. 281, 513-521.
107. Weng, Z., Rickles, R. J., Feng, S., Richard, S., Shaw, A. S., Schreiber, S. L., and Brugge, J. S. (1995). Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions. Mol. Cell. Biol. 15, 5627-5634.
108. Maignan, S., Guilloteau, J. P., Fromage, N., Arnoux, B., Becquart, J., and Ducruix, A. (1995). Crystal structure of the mammalian Grb2 adaptor. Science 268, 291-293.
109. Odai, H., Sasaki, K., Iwamatsu, A., Hanazono, Y., Tanaka, T., Mitani, K., Yazaki, Y., and Hirai, H. (1995). The proto-oncogene product c-Cbl becomes tyrosine phosphorylated by stimulation with GM-CSF or Epo and constitutively binds to the SH3 domain of Grb2/Ash in human hematopoietic cells. J. Biol. Chem. 270, 10800-10805.
110. Chen, J. K., Lane, W. S., Brauer, A., Tanaka, A., and Schreiber, S. L. (1993). Biased combinatorial libraries: Novel ligands for the SH3 domain of phosphatidylinositol 3-kinase. J. Am. Chem. Soc. 115, 12591-12592.
111. Goudreau, N., Cornille, F., Duchesne, M., Parker, F., Tocque, B., Garbay, C., and Roques, B. P. (1994). NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos. Nat. Struct. Biol. 1, 898-907.
112. Terasawa, H., Kohda, D., Hatanaka, H., Tsuchiya, S., Ogura, K., Nagata, K., Ishii, S., Mandiyan, V., Ullrich, A., Schlessinger, J., et al. (1994). Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos. Nat. Struct. Biol. 1, 891-897.
113. Wittekind, M., Mapelli, C., Farmer, B. T., II Suen, K. L., Goldfarb, V., Tsao, J., Lavoie, T., Barbacid, M., Meyers, C. A., and Mueller, L. (1994). Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy. Biochemistry 33, 13531-13539.
114. Feller, S. M., Posern, G., Voss, J., Kardinal, C., Sakkab, D., Zheng, J., and Knudsen, B. S. (1998). Physiological signals and oncogenesis mediated through Crk family adapter proteins. J. Cell Physiol. 177, 535-552.
115. Knudsen, B. S., Feller, S. M., and Hanafusa, H. (1994). Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk. J. Biol. Chem. 269, 32781-32787.
116. Tanaka, S., Morishita, T., Hashimoto, Y., Hattori, S., Nakamura, S., Shibuya, M., Matuoka, K., Takenawa, T., Kurata, T., Nagashima, K., et al. (1994). C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins. Proc. Natl. Acad. Sci. USA 91, 3443-3447.
117. Knudsen, B. S., Zheng, J., Feller, S. M., Mayer, J. P., Burrell, S. K., Cowburn, D., and Hanafusa, H. (1995). Affinity and specificity requirements for the first Src homology 3 domain of the Crk proteins. EMBO J. 14, 2191-2198.
118. Saksela, K., Cheng, G., and Baltimore, D. (1995). Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4. EMBO J. 14, 484-491.
119. Cullen, B. R. (1998). HIV-1 auxiliary proteins: Making connections in a dying cell. Cell 93, 685-692.
120. Lee, C. H., Leung, B., Lemmon, M. A., Zheng, J., Cowburn, D., Kuriyan, J., and Saksela, K. (1995). A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein. EMBO J. 14, 5006-5015.
121. Arold, S., O'Brien, R., Franken, P, Strub, M. P., Hoh, F., Dumas, C., and Ladbury, J. E. (1998). RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef. Biochemistry 37, 14683-14691.
122. Arold, S., Franken, P., Strub, M. P., Hoh, F., Benichou, S., Benarous, R., and Dumas, C. (1997). The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. Structure 5, 1361-1372.
123. Lim, W. A. (1996). Reading between the lines: SH3 recognition of an intact protein. Structure 4, 657-659.
124. Collette, Y., Arold, S., Picard, C., Janvier, K., Benichou, S., Benarous, R., Olive, D., and Dumas, C. (2000). HIV-2 and SIV nef proteins target different Src family SH3 domains than does HIV-1 Nef because of a triple amino acid substitution. J. Biol. Chem. 275, 4171-4176.
125. Hiipakka, M., Poikonen, K., and Saksela, K. (1999). SH3 domains with high affinity and engineered ligand specificities targeted to HIV-1 Nef. J. Mol. Biol. 293, 1097-1106.
126. Grzesiek, S., Bax, A., Clore, G. M., Gronenborn, A. M., Hu, J. S., Kaufman, J., Palmer, I., Stahl, S. J., and Wingfield, P. T. (1996). The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nat. Struct. Biol. 3, 340-345.
127. Laird, A. D., and Shalloway, D. (1997). Oncoprotein signalling and mitosis. Cell Signal. 9, 249-255.
128. Brown, M. T., and Cooper, J. A. (1996). Regulation, substrates and functions of src. Biochim. Biophys. Acta. 1287, 121-149.
129. Kato, J. Y., Takeya, T., Grandori, C., Iba, H., Levy, J. B., and Hanafusa, H. (1986). Amino acid substitutions sufficient to convert the nontransforming p60c-src protein to a transforming protein. Mol. Cell. Biol. 6, 4155-4160.
130. Potts, W. M., Reynolds, A. B., Lansing, T. J., and Parsons, J. T. (1988). Activation of pp60c-src transforming potential by mutations altering the structure of an amino terminal domain containing residues 90-95. Oncogene Res. 3, 343-355.
131. Murphy, S. M., Bergman, M., and Morgan, D. O. (1993). Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: Analysis with Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 5290-5300.
132. Superti-Furga, G., Fumagalli, S., Koegl, M., Courtneidge, S. A., and Draetta, G. (1993). Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src. EMBO J. 12, 2625-2634.
133. Okada, M., Howell, B. W., Broome, M. A., and Cooper, J. A. (1993). Deletion of the SH3 domain of Src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine. J. Biol. Chem. 268, 18070-18075.
134. Erpel, T., Superti-Furga, G., and Courtneidge, S. A. (1995). Mutational analysis of the Src SH3 domain: The same residues of the ligand binding surface are important for intra-and intermolecular interactions. EMBO J. 14, 963-975.
135. Xu, W., Doshi, A., Lei, M., Eck, M. J., and Harrison, S. C. (1999). Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol. Cell 3, 629-638.
136. Superti-Furga, G., and Gonfloni, S. (1997). A crystal milestone: The structure of regulated Src. Bioessays 19, 447-450.
137. Sicheri, F., and Kuriyan, J. (1997). Structures of Src-family tyrosine kinases. Curr. Opin. Struct. Biol. 7, 777-785.
138. Pawson, T. (1997). New impressions of Src and Hck. Nature 385, 582-585.
139. Nguyen, J. T., and Lim, W. A. (1997). How Src exercises self-restraint. Nat. Struct. Biol. 4, 256-260.
140. Mayer, B. J. (1997). Signal transduction: Clamping down on Src activity. Curr. Biol. 7, R295-R298.
141. Shalloway, D., and Taylor, S. J. (1997). Src: More than the sum of its parts. Trends Cell Biol. 7, 215-217.
142. Williams, J. C., Wierenga, R. K., and Saraste, M. (1998). Insights into Src kinase functions: Structural comparisons. Trends Biochem. Sci. 23, 179-184.
143. Young, M. A., Gonfloni, S., Superti-Furga, G., Roux, B., and Kuriyan, J. (2001). Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 105, 115-126.
144. Pellicena, P., and Miller, W. T. (2001). Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions. J. Biol. Chem. 276, 28190-28196.
145. Scott, M. P., and Miller, W. T. (2000). A peptide model system for processive phosphorylation by Src family kinases. Biochemistry 39, 14531-14537.
146. Moarefi, I., LaFevre-Bernt, M., Sicheri, F., Huse, M., Lee, C. H., Kuriyan, J., and Miller, W. T. (1997). Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 385, 650-653.
147. Gonfloni, S., Williams, J. C., Hattula, K., Weijland, A., Wierenga, R. K., and Superti-Furga, G. (1997). The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J. 16, 7261-7271.
148. Gonfloni, S., Frischknecht, F., Way, M., and Superti-Furga, G. (1999). Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis. Nat. Struct. Biol. 6, 760-764.
149. LaFevre-Bernt, M., Sicheri, F., Pico, A., Porter, M., Kuriyan, J., and Miller, W. T. (1998). Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue. J. Biol. Chem. 273, 32129-32134.
150. Gonfloni, S., Weijland, A., Kretzschmar, J., and Superti-Furga, G. (2000). Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src. Nat. Struct. Biol. 7, 281-286.
151. Barila, D., and Superti-Furga, G. (1998). An intramolecular SH3-domain interaction regulates c-Abl activity. Nat. Genet. 18, 280-282.
152. Bunnell, S. C., Henry, P. A., Kolluri, R., Kirchhausen, T., Rickles, R. J., and Berg, L. J. (1996). Identification of Itk/Tsk Src homology 3 domain ligands. J. Biol. Chem. 271, 25646-25656.
153. Andreotti, A. H., Bunnell, S. C., Feng, S., Berg, L. J., and Schreiber, S. L. (1997). Regulatory intramolecular association in a tyrosine kinase of the Tec family. Nature 385, 93-97.
154. Harpur, A. G., Layton, M. J., Das, P., Bottomley, M. J., Panayotou, G., Driscoll, P. C., and Waterfield, M. D. (1999). Intermolecular interactions of the p85alpha regulatory subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 274, 12323-12332.
155. Musacchio, A., Cantley, L. C., and Harrison, S. C. (1996). Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit. Proc. Natl. Acad. Sci. USA 93, 14373-14378.
156. McGee, A. W., and Bredt, D. S. (1999). Identification of an intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95. J. Biol. Chem. 274, 17431-17436.
157. Shin, H., Hsueh, Y. P., Yang, F. C., Kim, E., and Sheng, M. (2000). An intramolecular interaction between Src homology 3 domain and guanylate kinase-like domain required for channel clustering by postsynaptic density-95/SAP90. J. Neurosci. 20, 3580-3587.
158. Woods, D. F., Hough, C., Peel, D., Callaini, G., and Bryant, P. J. (1996). Dlg protein is required for junction structure, cell polarity, and proliferation control in Drosophila epithelia. J. Cell Biol. 134, 1469-1482.
159. Wu, H., Reissner, C., Kuhlendahl, S., Coblentz, B., Reuver, S., Kindler, S., Gundelfinger, E. D., and Garner, C. C. (2000). Intramolecular interactions regulate SAP97 binding to GKAP. EMBO J. 19, 5740-5751.
160. Nix, S. L., Chishti, A. H., Anderson, J. M., and Walther, Z. (2000). hCASK and hDIg associate in epithelia, and their src homology 3 and guanylate kinase domains participate in both intramolecular and intermolecular interactions. J. Biol. Chem. 275, 41192-41200.
161. Kato, M., Miyazawa, K., and Kitamura, N. (2000). A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP. J. Biol. Chem. 275, 37481-37487.
162. Kang, H., Freund, C., Duke-Cohan, J. S., Musacchio, A., Wagner, G., and Rudd, C. E. (2000). SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55. EMBO J. 19, 2889-2899.
163. Urquhart, A. J., Kennedy, D., Gould, S. J., and Crane, D. I. (2000). Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p. J. Biol. Chem. 275, 4127-4136.
164. Barnett, P., Bottger, G., Klein, A. T., Tabak, H. F., and Distel, B. (2000). The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction. EMBO J. 19, 6382-6391.
165. Scita, G., Nordstrom, J., Carbone, R., Tenca, P., Giardina, G., Gutkind, S., Bjarnegard, M., Betsholtz, C., and Di Fiore, P. P. (1999). EPS8 and E3B1 transduce signals from Ras to Rac. Nature 401, 290-293.
166. Kaelin, W. G., Jr. (1999). The p53 gene family. Oncogene 18, 7701-7705.
167. Iwabuchi, K., Bartel, P. L., Li, B., Marraccino, R., and Fields, S. (1994). Two cellular proteins that bind to wild-type but not mutant p53. Proc. Natl. Acad. Sci. USA 91, 6098-6102.
168. Cho, Y., Gorina, S., Jeffrey, P. D., and Pavletich, N. P. (1994). Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations. Science 265, 346-355.
169. Cho, Y., Gorina, S., Jeffrey, P. D., and Pavletich, N. P. (1994). Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations. Science 265, 346-355.
170. Nishida, M., Nagata, K., Hachimori, Y., Horiuchi, M., Ogura, K., Mandiyan, V., Schlessinger, J., and Inagaki, F. (2001). Novel recognition mode between Vav and Grb2 SH3 domains. EMBO J. 20, 2995-3007.
171. Park, H., Wahl, M. I., Afar, D. E., Turck, C. W., Rawlings, D. J., Tam, C., Scharenberg, A. M., Kinet, J. P., and Witte, O. N. (1996). Regulation of Btk function by a major autophosphorylation site within the SH3 domain. Immunity 4, 515-525.
172. Morrogh, L. M., Hinshelwood, S., Costello, P., Cory, G. O., and Kinnon, C. (1999). The SH3 domain of Bruton's tyrosine kinase displays altered ligand binding properties when auto-phosphorylated in vitro. Eur. J. Immunol. 29, 2269-2279.
173. Zhao, Z., Manser, E., and Lim, L. (2000). Interaction between PAK and
174. Rozakis-Adcock, M., van der Geer, P., Mbamalu, G., and Pawson, T. (1995). MAP kinase phosphorylation of mSos1 promotes dissociation of mSos1-Shc and mSos1-EGF receptor complexes. Oncogene 11, 1417-1426.
175. Corbalan-Garcia, S., Yang, S. S., Degenhardt, K. R., and Bar-Sagi, D. (1996). Identification of the mitogen-activated protein kinase phosphorylation sites on human Sos1 that regulate interaction with Grb2. Mol. Cell. Biol. 16, 5674-5682.
176. Bedford, M. T., Frankel, A., Yaffe, M. B., Clarke, S., Leder, P., and Richard, S. (2000). Arginine methylation inhibits the binding of proline-rich ligands to src homology 3, but not WW, domains. J. Biol. Chem. 275, 16030-16036.
177. Huang, J., and Kleinberg, M. E. (1999). Activation of the phagocyte NADPH oxidase protein p47(phox). Phosphorylation controls SH3 domain-dependent binding to p22(phox). J. Biol. Chem. 274, 19731-19737.
178. Hinshaw, J. E. (2000). Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 16, 483-519.
179. Nonoyama, S., and Ochs, H. D. (1998). Characterization of the Wiskott-Aldrich syndrome protein and its role in the disease. Curr. Opin. Immunol. 10, 407-412.
180. Sever, S., Damke, H., and Schmid, S. L. (2000). Garrotes, springs, ratchets, and whips: Putting dynamin models to the test. Traffic 1, 385-392.
181. Okamoto, P. M., Herskovits, J. S., and Vallee, R. B. (1997). Role of the basic, prolinerich region of dynamin in Src homology 3 domain binding and endocytosis. J. Biol. Chem. 272, 11629-11635.
182. Gout, I., Dhand, R., Hiles, I. D., Fry, M. J., Panayotou, G., Das, P., Truong, O., Totty, N. F., Hsuan, J., Booker, G. W., et al. (1993). The GTPase dynamin binds to and is activated by a subset of SH3 domains. Cell 75, 25-36.
183. Shupliakov, O., Low, P., Grabs, D., Gad, H., Chen, H., David, C., Takei, K., De Camilli, P., and Brodin, L. (1997). Synaptic vesicle endocytosis impaired by disruption of dynamin-SH3 domain interactions. Science 276, 259-263.
184. Morton, C. J., and Campbell, I. D. (1994). SH3 domains: Molecular 'Velcro.' Curr. Biol. 4, 615-617.
185. Kuriyan, J., and Cowburn, D. (1997). Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26, 259-288.
186. Moarefi, I., LaFevre-Bernt, M., Sicheri, F., Huse, M., Lee, C. H., Kuriyan, J., and Miller, W. T. (1997). Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 385, 650-653.
187. Dalgarno, D. C., Botfield, M. C., and Rickles, R. J. (1997). SH3 domains and drug design: Ligands, structure, and biological function. Biopolymers 43, 383-400.
188. Kardinal, C., Konkol, B., Schulz, A., Posern, G., Lin, H., Adermann, K., Eulitz, M., Estrov, Z., Talpaz, M., Arlinghaus, R. B., and Feller, S. M. (2000). Cell-penetrating SH3 domain blocker peptides inhibit proliferation of primary blast cells from CML patients. FASEB J. 14, 1529-1538.
189. Schumacher, T. N., Mayr, L. M., Minor, D. L., Jr., Milhollen, M. A., Burgess, M. W., and Kim, P. S. (1996). Identification of D-peptide ligands through mirror-image phage display. Science 271, 1854-1857.
190. Combs, A. P., Kapoort, T. M., Feng, S., Chen, J. K., Daude-Snow, L. F., and Schreiber, S. L. (1996). Protein structure-based combinatorial chemistry: Discovery of non-peptide binding elements to Src SH3 domain. J. Am. Chem. Soc. 118, 287-288.
191. Feng, S., and Schreiber, S. L. (1997). Enantiomeric binding elements interacting at the same site of an SH3 protein receptor. J. Am. Chem. Soc. 119, 10873-10874.
192. Morken, J. P., Kapoor, T. M., Feng, S., Shirai, F., and Schreiber, S. L. (1998). Exploring the leucine-proline binding pocket of the Src SH3 domain using structure-based, split-pool synthesis and affinity-based selection. J. Am. Chem. Soc. 120, 30-36.
193. Kapoor, T. M., Andreotti, A. H., and Schreiber, S. L. (1998). Exploring the specificity pockets of two homologous SH3 domains using structure-based, split-pool synthesis and affinity-based selection. J. Am. Chem. Soc. 120, 23-29.
194. Barfod, E. T., Zheng, Y., Kuang, W. J., Hart, M. J., Evans, T., Cerione, R. A., and Ashkenazi, A. (1993). Cloning and expression of a human CDC42 GTPase-activating protein reveals a functional SH3-binding domain. J. Biol. Chem. 268, 26059-26062.
195. Weng, Z., Thomas, S. M., Rickles, R. J., Taylor, J. A., Brauer, A. W., Seidel-Dugan, C., Michael, W. M., Dreyfuss, G., and Brugge, J. S. (1994). Identification of Src, Fyn, and Lyn SH3-binding proteins: Implications for a function of SH3 domains. Mol. Cell. Biol. 14, 4509-4521.
196. Kapeller, R., Prasad, K. V., Janssen, O., Hou, W., Schaffhausen, B. S., Rudd, C. E., and Cantley, L. C. (1994). Identification of two SH3-binding motifs in the regulatory subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 269, 1927-1933.
197. Holmes, T. C., Fadool, D. A., Ren, R., and Levitan, I. B. (1996). Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain. Science 274, 2089-2091.
198. Nakamoto, T., Sakai, R., Ozawa, K., Yazaki, Y., and Hirai, H. (1996). Direct binding of C-terminal region of p130Cas to SH2 and SH3 domains of Src kinase. J. Biol. Chem. 271, 8959-8965.
199. Alexandropoulos, K., Cheng, G., and Baltimore, D. (1995). Proline-rich sequences that bind to Src homology 3 domains with individual specificities. Proc. Natl. Acad. Sci. USA 92, 3110-3114.
200. Karlsson, T., Songyang, Z., Landgren, E., Lavergne, C., Di Fiore, P. P., Anafi, M., Pawson, T., Cantley, L. C., Claesson-Welsh, L., and Welsh, M. (1995). Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins. Oncogene 10, 1475-1483.
201. Onofri, F., Giovedi, S., Vaccaro, P., Czernik, A. J., Valtorta, F., De Camilli, P., Greengard, P., and Benfenati, F. (1997). Synapsin I interacts with c-Src and stimulates its tyrosine kinase activity. Proc. Natl. Acad. Sci. USA 94, 12168-12173.
202. Weng, Z., Taylor, J. A., Turner, C. E., Brugge, J. S., and Seidel-Dugan, C. (1993). Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells. J. Biol. Chem. 268, 14956-14963.
203. Flynn, D. C., Leu, T. H., Reynolds, A. B., and Parsons, J. T. (1993). Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp60src substrate. Mol. Cell. Biol. 13, 7892-7900.
204. Cheng, G., Ye, Z. S., and Baltimore, D. (1994). Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction. Proc. Natl. Acad. Sci. USA 91, 8152-8155.
205. Li, E., Stupack, D. G., Brown, S. L., Klemke, R., Schlaepfer, D. D., and Nemerow, G. R. (2000). Association of p130CAS with phosphatidylinositol-3-OH kinase mediates adenovirus cell entry. J. Biol. Chem. 275, 14729-14735.
206. Manser, E., Loo, T. H., Koh, C. G., Zhao, Z. S., Chen, X. Q., Tan, L., Tan, I., Leung, T., and Lim, L. (1998). PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. Mol. Cell 1, 183-192.
207. Sudol, M. (1994). Yes-associated protein (YAP65) is a proline-rich phosphoprotein that binds to the SH3 domain of the Yes proto-oncogene product. Oncogene 9, 2145-2152.
208. Glover, R. T., Angiolieri, M., Kelly, S., Monaghan, D. T., Wang, J. Y., Smithgall, T. E., and Buller, A. L. (2000). Interaction of the N-methyl-D-aspartic acid receptor NR2D subunit with the c-Abl tyrosine kinase. J. Biol. Chem. 275, 12725-12729.
209. Shafman, T., Khanna, K. K., Kedar, P., Spring, K., Kozlov, S., Yen, T., Hobson, K., Gatei, M., Zhang, N., Watters, D., Egerton, M., Shiloh, Y., Kharbanda, S., Kufe, D., and Lavin, M. F. (1997). Interaction between ATM protein and c-Abl in response to DNA damage. Nature 387, 520-523.
210. Majidi, M., Hubbs, A. E., and Lichy, J. H. (1998). Activation of extracellular signal-regulated kinase 2 by a novel Abl-binding protein, ST5. J. Biol. Chem. 273, 16608-16614.
211. Ren, R., Ye, Z. S., and Baltimore, D. (1994). Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites. Genes Dev. 8, 783-794.
212. Schumacher, C., Knudsen, B. S., Ohuchi, T., Di Fiore, P. P., Glassman, R. H., and Hanafusa, H. (1995). The SH3 domain of Crk binds specifically to a conserved prolinerich motif in Eps15 and Eps15R. J. Biol. Chem. 270, 15341-15347.
213. Wang, B., Mysliwiec, T., Feller, S. M., Knudsen, B., Hanafusa, H., and Kruh, G. D. (1996). Proline-rich sequences mediate the interaction of the Arg protein tyrosine kinase with Crk. Oncogene 13, 1379-1385.
214. Bokoch, G. M., Wang, Y., Bohl, B. P., Sells, M. A., Quilliam, L. A., and Knaus, U. G. (1996). Interaction of the Nck adapter protein with p21-activated kinase (PAK1). J. Biol. Chem. 271, 25746-25749.
215. Galisteo, M. L., Chernoff, J., Su, Y. C., Skolnik, E. Y., and Schlessinger, J. (1996). The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1. J. Biol. Chem. 271, 20997-21000.
216. Anton, I. M., Lu, W., Mayer, B. J., Ramesh, N., and Geha, R. S. (1998). The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck. J. Biol. Chem. 273, 20992-20995.
217. Wu, Y., Dowbenko, D., and Lasky, L. A. (1998). PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase. J. Biol. Chem. 273, 30487-30496.
218. Rivero-Lezcano, O. M., Sameshima, J. H., Marcilla, A., and Robbins, K. C. (1994). Physical association between Src homology 3 elements and the protein product of the c-cbl proto-oncogene. J. Biol. Chem. 269, 17363-17366.
219. Carlier, M. F., Nioche, P., Broutin-L'Hermite, I., Boujemaa, R., Le Clainche, C., Egile, C., Garbay, C., Ducruix, A., Sansonetti, P. J., and Pantaloni, D. (2000). GRB2 links signalling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-Wasp) with actin-related-protein (ARP2/3) complex. J. Biol. Chem 275, 21946-21952.
220. Finan, P., Shimizu, Y., Gout, I., Hsuan, J., Truong, O., Butcher, C., Bennett, P., Waterfield, M. D., and Kellie, S. (1994). An SH3 domain and proline-rich sequence mediate an interaction between two components of the phagocyte NADPH oxidase complex. J. Biol. Chem. 269, 13752-13755.
221. Harte, M. T., Hildebrand, J. D., Burnham, M. R., Bouton, A. H., and Parsons, J. T. (1996). p130Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase. J. Biol. Chem. 271, 13649-13655.
222. Hansson, H., Mattsson, P. T., Allard, P., Haapaniemi, P., Vihinen, M., Smith, C. I., and Hard, T. (1998). Solution structure of the SH3 domain from Bruton's tyrosine kinase. Biochemistry 37, 2912-2924.
223. Borchert, T. V., Mathieu, M., Zeelen, J. P., Courtneidge, S. A., and Wierenga, R. K. (1994). The crystal structure of human CskSH3: Structural diversity near the RT-Src and n-Src loop. FEBS Lett. 341, 79-85.
224. Kohda, D., Terasawa, H., Ichikawa, S., Ogura, K., Hatanaka, H., Mandiyan, V., Ullrich, A., Schlessinger, J., and Inagaki, F. (1994). Solution structure and ligand-binding site of the carboxy-ferminal SH3 domain of GRB2. Structure 2, 1029-1040.
225. Politou, A. S., Millevoi, S., Gautel, M., Kolmerer, B., and Pastore, A. (1998). SH3 in muscles: Solution structure of the SH3 domain from nebulin. J. Mol. Biol. 276, 189-202.
226. Liang, J., Chen, J. K., Schreiber, S. T., and Clardy, J. (1996). Crystal structure of PI3K SH3 domain at 2.0 angstroms resolution. J. Mol. Biol. 257, 632-643.
227. Viguera, A. R., Blanco, F. J., and Serrano, L. (1995). The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J. Mol. Biol. 247, 670-681.
228. 15N NMR assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure. J. Biomol. NMR 9, 347-357.
229. Martinez, J. C., Pisabarro, M. T., and Serrano, L. (1998). Obligatory steps in protein folding and the conformational diversity of the transition state. Nat. Struct. Biol. 5, 721-729.
230. Gosser, Y. Q., Zheng, J., Overduin, M., Mayer, B. J., and Cowburn, D. (1995). The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct. Structure 3, 1075-1086.
231. Nam, H. J., Haser, W. G., Roberts, T. M., and Frederick, C. A. (1996). Intramolecular interactions of the regulatory domains of the Bcr-Abl kinase reveal a novel control mechanism. Structure 4, 1105-1114.
232. Eck, M. J., Atwell, S. K., Shoelson, S. E., and Harrison, S. C. (1994). Structure of the regulatory domains of the Src-family tyrosine kinase Lck. Nature 368, 764-769.
233. Tzeng, S. R., Lou, Y. C., Pai, M. T., Jain, M. L., and Cheng, J. W. (2000). Solution structure of the human BTK SH3 domain complexed with a proline-rich peptide from p120cbl. J. Biomol. NMR 16, 303-312.
234. Horita, D. A., Baldisseri, D. M., Zhang, W., Altieri, A. S., Smithgall, T. E., Gmeiner, W. H., and Byrd, R. A. (1998). Solution structure of the human Hck SH3 domain and identification of its ligand binding site. J. Mol. Biol. 278, 253-265.
235. Carson, M. (1991). Ribbons 2.0. J. Appl. Crystallogr. 24, 958-961.
236. Nicholls, A., Sharp, K. A., and Honig, B. (1991). Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.