pH-dependent self-association of the Src homology 2 (SH2) domain of the Src homologous and collagen-like (SHC) protein

Protein Science

Volumn 5, Issue 3, 1996, Pages 405-413

  Réty, Stéphane ^a   Fütterer, Klaus ^a   Grucza, Richard A ^a   Munoz, Consuelo M ^a   Frazier, William A ^a   Waksman, Gabriel ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

crystal structure; sedimentation equilibrium; self association; SH2; SHC

Indexed keywords

T LYMPHOCYTE RECEPTOR;

AMINO ACID SEQUENCE; ARTICLE; COLLAGEN METABOLISM; CRYSTAL STRUCTURE; DIMERIZATION; DISULFIDE BOND; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

EID: 0029878111     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050301     Document Type: Article

References (46)

1. Booker GW, Breeze AL, Downing AK, Panayotou G, Gout I, Waterfield MD, Campbell ID. 1992. Structure of an SH2 domain of the p85α subunit of phosphatidylinositol-3-OH kinase Nature 358:684-687.
2. Booker GW, Gout I, Downing AK, Driscoll PC, Boyd J, Waterfield MD, Campbell ID. 1993. Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3 kinase Cell 73: 813-822.
3. Bork P, Margolis B. 1995. A phosphotyrosine interaction domain. Cell 80: 693-694.
4. Brunger AT. 1988. X-PLOR manual. New Haven, Connecticut: Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University.
5. CCP4. 1994. Collaborative computational project number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763.
6. Cohn EJ, Edsall JT. 1943. Proteins, ammo acids and peptides as ions and dipolar ions. New York: Rheinhold.
7. lck. Nature 362:87-91.
8. Eck MJ, Atwell SK, Shoelson SE, Harrison SC. 1994. Structure of the regulatory domains of the Src-family tyrosine kinase Lck. Nature 368: 764-769.
9. Fulton AB. 1982. How crowded is the cytoplasm. Cell 30:345-347.
10. Gill SC, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid data. Anal Biochem 182:319-326.
11. Hendrickson WA, Horton JR, LeMaster D. 1990. Selenomethionine proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. EMBO J 9:1665-1672.
12. Hodel A, Kim SH, Brünger AT. 1992. Model bias in crystal structures. Acta Crystallogr A 48:851-858.
13. Janin J, Chothia C. 1990. The structure of protein-protein recognition sites. J Biol Chem 265:16027-16030
14. Johnson ML, Correira JJ, Yphantis DA, Halvorson HR. 1981. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys J 36:575-588.
15. Jones TA, Thirup S 1986. Using known substructures in protein model building and crystallography. EMBO J 5:819-822.
16. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
17. Kavanaugh WM, Williams LT. 1994. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266:1862-1865.
18. Koch CA, Anderson D, Moran MF, Ellis C, Pawson T. 1991. SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins. Science 252:668-674.
19. Kraulis PJ. 1991. MOLSCRIPT: A program to reproduce both detailed and schematic plots of protein structure. J Appl Crysiallogr 24:946-950.
20. Laue TM, Shah BD, Ridgeway TM, Pelletier SL. 1992 Computer-aided interpretation of analytical sedimentation data for proteins. In: Hardy S, Rowe, A, Horton JC, eds. Analytical ultracentrifugation in biochemistry and polymer science. London: Royal Society of Chemistry, pp 90-125.
21. Lee CH, Kominos D, Jacques S, Margolis B, Schlessinger J, Shoelson SE, Kuriyan J. 1994. Costal structure of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase. Structure 2:423-438.
22. Lemmon MA, Schlessinger J. 1994. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem Sci 19:459-463.
23. Maignan S, Guilloteau JP, Fromage N, Arnoux B, Becquart J, Ducruix A. 1995. Crystal structure of the mammalian GRB2 adaptor. Science 268: 291-293.
24. Marengere LE, Songyang Z, Gish CD, Schaffer MD, Parsons JT, Stern MJ, Cantley LC, Pawson T. 1994. SH2 domain specificity and activity modified by a single residue. Nature 369:502-505.
25. Marengere LEM, Pawson T. 1992. Identification of residues in GTPase activating protein Src homology 2 domains that control binding to tyrosine phosphorylated growth factor receptors and p62. J Biol Chem 267: 22779-22786.
26. McDonald IK, Thornton JM. 1994. Satisfying hydrogen bonding potential in proteins. J Mol Biol 238:777-793.
27. McPherson A. 1990. Current approaches to macromolecular crystallization. Eur J Biochem 189:1-23.
28. Mikol V, Baumann G, Zurini MGM, Hommel U. 1995. Crystal structure of the SH2 domain from the adaptor protein SHC: A model for peptide binding based on X-ray and NMR data. J Mol Biol 254:86-95.
29. Minton AP, Wilf J. 1981. Effect of macromolecular crowding upon the structure and function of an enzyme: Glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 20:4621-4626.
30. Navaza J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr A 50:157-163.
31. Nicholas A, Sharp KA, Honig B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Protein Struct Funct Genet 11:281-296.
32. Pascal S, Singer AU, Gish G, Yamazaki T, Shoelson SE, Pawson T, Kay LE, Forman-Kay JD. 1994. Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-γ1 complexed with a high affinity binding peptide. Cell 77:461-472.
33. Pelicci G, Lanfrancone L, Grignani F, McGlade J, Cavallo F, Forni G, Nicoletti L, Grignani F, Pawson T, Pelicci PG. 1992. A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell 70:93-104.
34. Prats M, Teissie J, Tocanne JF. 1986. Lateral proton conduction at lipid-water interfaces and its implications for the chemiosmotic-coupling hypothesis. Nature 522:756-758.
35. Read R. 1986. Improved coefficients for maps using phases from partial structures with errors. Acta Crystallogr A 42:140-149.
36. Richards FM. 1977 Areas, volumes, packing, and protein structure. Annu Rev Biophys Bioeng 6:151-176.
37. Rozakis-Adcock M, McGlade J, Mbamalu G, Pelicci G, Daly R, Li W, Batzer A, Thomas S, Brugge J, Pelicci PG, Schlessinger J, Pawson T. 1992. Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway of tyrosine kinases. Nature 360: 689-692.
38. Songyang Z, Shoelson SE, McGlade J, Olivier P, Pawson T, Bustelo XR, Barbacid M, Sabe H, Hanafusa H, Yi T, Ren R, Baltimore D, Ratnofski S, Feldman RA, Cantley LC. 1994. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, Vav. Mol Cell Biol 14:2777-2785.
39. van der Geer P, Pawson T. 1995. The PTB domain: A new protein module implicated in signal transduction. Trends Biochem Sci 20:277-280.
40. Waksman G, Kominos D, Robertson SR, Pant N, Baltimore D, Birge RB, Cowburn D, Hanafusa H, Mayer BJ, Overduin M, Resh MD, Rios CB, Silverman L, Kuriyan J. 1992. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature 358:646-653
41. Waksman G, Krishna TSR, Williams CH, Kuriyan J. 1994. Crystal structure of Escherichia coli thioredoxin reductase refined at 2 Å resolution. J Mol Biol 256:800-816.
42. Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J. 1993. Binding of a high affinity phosphotyrosyl peptide to the src SH2 domain: Crystal structures of the complexed and peptide-free forms. Cell 72:779-790.
43. Weng Z, Thomas SM, Rickles RJ, Taylor JA, Brauer AW, Seidel-Dugan C, Michael WM, Dreyfuss G, Brugge JS. 1994. Identification of Src, Fyn, and Lyn SH3-binding proteins: Implications for a function of SH3 domains. Mol Cell Biol 14:4509-4521.
44. Wilf J, Minton AP. 1981. Evidence for protein self-association induced by excluded volume. Myoglobin in the presence of globular proteins. Biochem Biophys Acta 670:316-322.
45. Ye ZS, Baltimore D. 1994. Binding of Vav to Grb2 through dimerization of Src homology 3 domains. Proc Natl Acad Sci USA 91:12629-12633.
46. Zhou MM, Meadous RP, Logan TM, Yoon HS, Wade WS, Ravichandran K, Burakoff SJ, Fesik SW. 1995. Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. Proc Natl Acad Sci USA 92:7784-7788.