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Volumn 391, Issue 1, 2010, Pages 33-42

Structural studies of the phosphatidylinositol 3-kinase (PI3K) SH3 domain in complex with a peptide ligand: Role of the anchor residue in ligand binding

Author keywords

stacking; Phosphatidylinositol 3 kinase; Polyproline helix; Protein ligand interaction; Src homology 3

Indexed keywords

ARGININE; PEPTIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN SH3; TRYPTOPHAN; TYROSINE;

EID: 75149184920     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2010.003     Document Type: Article
Times cited : (16)

References (42)
  • 2
    • 0027191192 scopus 로고
    • Solution structure and ligand-binding site of the SH3 domain of the p85 a subunit of phosphatidylinositol 3-kinase
    • 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 a subunit of phosphatidylinositol 3-kinase. Cell 73, 813-822.
    • (1993) Cell , vol.73 , pp. 813-822
    • Booker, G.W.1    Gout, I.2    Downing, A.K.3    Driscoll, P.C.4    Boyd, J.5    Waterfield, M.D.6    Campbell, I.D.7
  • 4
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos, A.M., Ultsch, M., and Kossiakoff, A.A. (1992). Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 5
    • 0030219389 scopus 로고    scopus 로고
    • More on target with protein phosphorylation: Conferring specificity by location
    • Faux, M.C. and Scott, J.D. (1996). More on target with protein phosphorylation: conferring specificity by location. Trends Biochem. Sci. 21, 312-315.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 312-315
    • Faux, M.C.1    Scott, J.D.2
  • 6
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • 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.
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 7
    • 0347627529 scopus 로고    scopus 로고
    • The tryptophan switch: Changing ligand-binding specificity from type i to type II in SH3 domains
    • Fernandez-Ballester, G., Blanes-Mira, C., and Serrano, L. (2004). The tryptophan switch: changing ligand-binding specificity from type I to type II in SH3 domains. J. Mol. Biol. 335, 619-629.
    • (2004) J. Mol. Biol. , vol.335 , pp. 619-629
    • Fernandez-Ballester, G.1    Blanes-Mira, C.2    Serrano, L.3
  • 8
    • 0024461553 scopus 로고
    • Deletion of an Nterminal regulatory domain of the c-abl tyrosine kinase activates its oncogenic potential
    • Franz, W.M., Berger, P., and Wang, J.Y. (1989). Deletion of an Nterminal regulatory domain of the c-abl tyrosine kinase activates its oncogenic potential. EMBO J. 8, 137-147.
    • (1989) EMBO J , vol.8 , pp. 137-147
    • Franz, W.M.1    Berger, P.2    Wang, J.Y.3
  • 10
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S.K. and Hunter, T. (1995). Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 12
    • 0024343691 scopus 로고
    • N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl
    • Jackson, P. and Baltimore, D. (1989). N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl. EMBO J. 8, 449-456.
    • (1989) EMBO J , vol.8 , pp. 449-456
    • Jackson, P.1    Baltimore, D.2
  • 13
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 14
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 15
    • 0028151515 scopus 로고
    • Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527
    • Kaplan, K.B., Bibbins, K.B., Swedlow, J.R., Arnaud, M., Morgan D.O., and Varmus, H.E. (1994). Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J. 13, 4745-4756.
    • (1994) EMBO J , vol.13 , pp. 4745-4756
    • Kaplan, K.B.1    Bibbins, K.B.2    Swedlow, J.R.3    Arnaud, M.4    Morgan, D.O.5    Varmus, H.E.6
  • 16
    • 0035190026 scopus 로고    scopus 로고
    • Cellular function of phosphoinositide 3-kinases: Implications for development, homeostasis, and cancer
    • Katso, R., Okkenhaug, K., Ahmadi, K., White, S., Timms, J., and Waterfield, M.D. (2001). Cellular function of phosphoinositide 3-kinases: implications for development, homeostasis, and cancer. Annu. Rev. Cell Dev. Biol. 17, 615-675.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 615-675
    • Katso, R.1    Okkenhaug, K.2    Ahmadi, K.3    White, S.4    Timms, J.5    Waterfield, M.D.6
  • 18
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins
    • Koch, C.A., Anderson, D., Moran, M.F., Ellis, C., and Pawson, T. (1991). SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252, 668-674.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kuriyan, J. and Cowburn, D. (1997). Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 26, 259-288.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 22
    • 0034486070 scopus 로고    scopus 로고
    • The identification of conserved interactions within the SH3 domain by alignment of sequences and structures
    • 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.
    • (2000) Protein Sci , vol.9 , pp. 2170-2180
    • Larson, S.M.1    Davidson, A.R.2
  • 23
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data. Jnt. CCP4/ESFEAMCB Newslett
    • Leslie, A.G.W. (1992). Recent changes to the MOSFLM package for processing film and image plate data. Jnt. CCP4/ESFEAMCB Newslett. Protein Crystallogr. 26.
    • (1992) Protein Crystallogr , pp. 26
    • Leslie, A.G.W.1
  • 24
    • 0029980671 scopus 로고    scopus 로고
    • Crystal structure of P13K SH3 domain at 2 Å resolution
    • Liang, J., Chen, J.K., Schreiber, S.T., and Clardy, J. (1996). Crystal structure of P13K SH3 domain at 2 Å resolution. J. Mol. Biol. 257, 632-643.
    • (1996) J. Mol. Biol. , vol.257 , pp. 632-643
    • Liang, J.1    Chen, J.K.2    Schreiber, S.T.3    Clardy, J.4
  • 25
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • 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.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 28
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt, E.A. and Bacon, D.J. (1997). Raster3D photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 29
    • 0036420970 scopus 로고    scopus 로고
    • How SH3 domains recognize praline
    • Musacchio, A. (2002). How SH3 domains recognize proline. Adv. Protein Chem. 61, 211-268.
    • (2002) Adv. Protein Chem. , vol.61 , pp. 211-268
    • Musacchio, A.1
  • 30
    • 0026749753 scopus 로고
    • SH3: An abundant protein domain in search of a function
    • Musacchio, A., Gibson, T., Lehto, V.P., and Saraste, M. (1992). SH3: an abundant protein domain in search of a function. FEBS Lett. 307, 55-61.
    • (1992) FEBS Lett , vol.307 , pp. 55-61
    • Musacchio, A.1    Gibson, T.2    Lehto, V.P.3    Saraste, M.4
  • 31
    • 0025755422 scopus 로고
    • Characterization of two 85 kD proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase
    • Otsu, M., Hiles, I., Gout, I., Fry, M.J., Ruiz-Larrea, F., Panayotou, G., Thompson, A., Dhand, R., Hsuan, J., Totty, N., et al. (1991). Characterization of two 85 kD proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3- kinase. Cell 65, 91-104.
    • (1991) Cell , vol.65 , pp. 91-104
    • Otsu, M.1    Hiles, I.2    Gout, I.3    Fry, M.J.4    Ruiz-Larrea, F.5    Panayotou, G.6    Thompson, A.7    Dhand, R.8    Hsuan, J.9    Totty, N.10
  • 32
    • 0026484261 scopus 로고
    • SH2 and SH3 domains: From structure to function
    • Pawson, T. and Gish, G.D. (1992). SH2 and SH3 domains: from structure to function. Cell 71, 359-362.
    • (1992) Cell , vol.71 , pp. 359-362
    • Pawson, T.1    Gish, G.D.2
  • 34
    • 0030927326 scopus 로고    scopus 로고
    • Activation of the JNK pathway is essential for transformation by the Met oncogene
    • Rodrigues, G.A., Park, M., and Schlessinger, J. (1997). Activation of the JNK pathway is essential for transformation by the Met oncogene. EMBO J. 16, 2634-2645.
    • (1997) EMBO J , vol.16 , pp. 2634-2645
    • Rodrigues, G.A.1    Park, M.2    Schlessinger, J.3
  • 35
  • 36
    • 0025921611 scopus 로고
    • Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases
    • Skolnik, E.Y., Margolis, B., Mohammadi, M., Lowenstein, E., Fischer, R., Drepps, A., Ullrich, A., and Schlessinger, J. (1991). Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases. Cell 65, 83-90.
    • (1991) Cell , vol.65 , pp. 83-90
    • Skolnik, E.Y.1    Margolis, B.2    Mohammadi, M.3    Lowenstein, E.4    Fischer, R.5    Drepps, A.6    Ullrich, A.7    Schlessinger, J.8
  • 37
    • 34250012538 scopus 로고    scopus 로고
    • Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide
    • Stangler, T., Tran, T., Hoffmann, S., Schmidt, H., Jonas, E., and Willbold, D. (2007). Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide. Biol. Chem. 388, 611-615.
    • (2007) Biol. Chem. , vol.388 , pp. 611-615
    • Stangler, T.1    Tran, T.2    Hoffmann, S.3    Schmidt, H.4    Jonas, E.5    Willbold, D.6
  • 38
    • 1842431419 scopus 로고    scopus 로고
    • High-throughput structural biology in drug discovery: Protein kinases
    • Stout, T.J., Foster, P.G., and Matthews, D.J. (2004). High-throughput structural biology in drug discovery: protein kinases. Curr. Pharm. Des. 10, 1069-1082.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1069-1082
    • Stout, T.J.1    Foster, P.G.2    Matthews, D.J.3
  • 39
    • 0027182279 scopus 로고
    • Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src
    • 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.
    • (1993) EMBO J , vol.12 , pp. 2625-2634
    • Superti-Furga, G.1    Fumagalli, S.2    Koegl, M.3    Courtneidge, S.A.4    Draetta, G.5
  • 40
    • 27744568614 scopus 로고    scopus 로고
    • Insights into human Lck SH3 domain binding specificity: Different binding modes of artificial and native ligands
    • Tran, T., Hoffmann, S., Wiesehan, K., Jonas, E., Luge, C., Aladag, A., and Willbold, D. (2005). Insights into human Lck SH3 domain binding specificity: different binding modes of artificial and native ligands. Biochemistry 44, 15042-15052.
    • (2005) Biochemistry , vol.44 , pp. 15042-15052
    • Tran, T.1    Hoffmann, S.2    Wiesehan, K.3    Jonas, E.4    Luge, C.5    Aladag, A.6    Willbold, D.7
  • 42
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline-rich peptides to SH3 domains
    • 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.
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1    Chen, J.K.2    Feng, S.3    Dalgarno, D.C.4    Brauer, A.W.5    Schreiber, S.L.6


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