Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain

Nature Structural Biology

Volumn 3, Issue 4, 1996, Pages 388-393

  Zhou, Ming Ming ^a   Huang, Baohua ^a   Olejniczak, Edward T ^a   Meadows, Robert P ^a   Shuker, Suzanne B ^a   Miyazaki, Masaya ^b   Trüb, Thomas ^b   Shoelson, Steven E ^b   Fesik, Stephen W ^a  

^a ABBOTT LABORATORIES   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN; INSULIN RECEPTOR; INTERLEUKIN 4; INTERLEUKIN 4 RECEPTOR; PHOSPHOPEPTIDE; PHOSPHOTYROSINE;

ARTICLE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANTIGENS, CD; BINDING SITES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOSPHOPEPTIDES; PHOSPHOPROTEINS; PHOSPHOTYROSINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, INTERLEUKIN; RECEPTORS, INTERLEUKIN-4; SEQUENCE ALIGNMENT;

EID: 0029940882     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (33)

1. Myers, M.G., Jr, Sun, X.J. & White, M.F. The IRS-1 signaling system. Trends Biochem. Sci. 192, 89-293 (1994).
2. Sun, X.J. et al. Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein. Nature 352, 73-77 (1991).
3. Wang, L.-M. et al. IRS-1: Essential for insulin- and IL-4-stimulated mitogensis in hematopoietic cells. Science 261, 1591-1594 (1993).
4. Keegan, A.D. et al. An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth. Cell 76, 811-820 (1994).
5. Gustafson, T.A., He, W., Craparo, A., Schaub, C.D. & O'Neill, T.J. Phosphotyrosine-dependent interaction of Shc and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Mol. Cell. Biol. 15, 2500-2508 (1995).
6. Kavanaugh, W.M. & Williams, L.T. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266, 1862-1865 (1994).
7. Blaikie, P. et al. A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem. 269, 32031-32034 (1994).
8. van der Geer, P. et al. A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides. Current Biol. 5, 404-412 (1995).
9. Zhou, M.-M. et al. Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature 378, 584-592 (1995).
10. Trüb, T. et al. Specificity of the PTB domain of Shc for β turn forming pentapeptide motifs amino-terminal to phosphotyrosine. J. Biol. Chem. 270, 18205-18208 (1995).
11. Songyang, Z., Margolis, B., Chaudhuri, M., Shoelson, S.E. & Cantley, L.C. The phosphotyrosine interaction domain of Shc recognizes tyrosine-phosphorylated NPXY motif. J. Biol. Chem. 270, 14863-18466 (1995).
12. Wolf, G. et al. PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities. J. Biol. Chem. 270, 27407-27410 (1995).
13. Sun, X.J. et al. Role of IRS-2 in insulin and cytokine signalling. Nature 377, 173-177 (1995).
14. Kavanaugh, W.M., Turck, C.W. & Williams, L.T. PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 268, 1177-1180 (1995).
15. Yoon, H.S. et al. Solution structure of a pleckstrin-homology domain. Nature 369, 672-675 (1994).
16. Macias, M. J. et al. Structure of the pleckstrin homology domain from β-spectrin. Nature 369, 675-677 (1994).
17. Downing, A.K. et al. Three-dimensional solution structure of the pleckstrin homology domain from dynamin. Curr. Biol. 4, 884-891 (1994).
18. Ferguson, K.M., Lemmon, M.A., Schlessinger, J. & Sigler, P.B. Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin. Cell 79, 199-209 (1994).
19. Timm, D. et al. Crystal structure of the pleckstrin homology domain from dynamin Nature Struct. Biol. 1, 782-788 (1994).
20. Fushman, D., Cahill, S., Lemmon, M.A., Schlessinger, J. & Cowburn, D. Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy. Proc. Natl. Acad. Sci. USA 92, 816-820 (1995).
21. Zhang, P., Talluri, S., Deng, H., Branton, D. & Wagner, G. Solution structure of the pleckstrin homology domain of Drosophila β-spectrin. Structure 3, 1185-1195 (1995).
22. Ferguson, K.M., Lemmon, M.A., Schlessinger, J. & Sigler, P.B. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83, 1037-1046 (1995).
23. Harlan, J.E., Hajduk, P.J., Yoon, H.S. & Fesik, S.W. Pleckstrin homology domains bind to phosphatidylinosital 4,5-bisphosphate. Nature 371, 168-170 (1994).
24. Myers, M.G. Jr. et al. The pleckstrin homology domain in insulin receptor subrtrate-1 sensitizes insulin signaling. J. Biol. Chem. 270, 11715-11718 (1995).
25. Touhara, K. et al. Binding of G protein βγ-subunits to pleckstrin homology domains. J. Biol. Chem. 269, 10217-10220 (1994).
26. 2H labeled proteins with high sensitivity. J. Am. Chem. Soc. 116, 11655-11666 (1994).
27. Clore, G.M. & Gronenborn, A.M. Multidimensional heteronuclear nuclear magnetic resonance of proteins. Methods Enzymol. 239, 349-363 (1994).
28. Neri, D., Szyperski, T., Otting, G., Senn. H. & Wüthrich, K. Biochemistry 28, 7510-7516 (1989).
29. Nilges, M., Clore, G.M. & Gronenborn, A.M. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance goemetry-dynamical simulated annealing calculations. FEBS Lett. 229, 317-324 (1988).
30. Kuszewski, J., Nilges, M. & Brünger, A.T. A sampling and efficacy of metric matrix distance geometry: a novel partial metrization algorithm. J. Biomol. NMR 2, 33-56 (1992).
31. Brünger, A.T. X-PLOR Manual, Yale Univ. Press, Cambridge, MA, version 3.1 (1992).
32. Carson, M. Ribbons. J. Molec. Graphics 5, 103-106 (1987).
33. Brooks, B.R. et al. CHARMM: a program for macromolecular energy minimization, and dynamics calculations. J. Comput. Chem. 4, 187-217 (1983).