The Structure of a Receptor with Two Associating Transmembrane Domains on the Cell Surface: Integrin αIIbβ3

Molecular Cell

Volumn 34, Issue 2, 2009, Pages 234-249

  Zhu, Jieqing ^a   Luo, Bing Hao ^a   Barth, Patrick ^b   Schonbrun, Jack ^b   Baker, David ^b   Springer, Timothy A ^a  

^a BOSTON CHILDREN S HOSPITAL   (United States)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

PROTEINS; SIGNALING

Indexed keywords

DISULFIDE; INTEGRIN; INTEGRIN ALPHA2B BETA3; UNCLASSIFIED DRUG;

ARTICLE; CELL SURFACE; CROSS LINKING; CRYSTAL STRUCTURE; IMMUNOPRECIPITATION; LIGAND BINDING; MEMBRANE STRUCTURE; MUTATIONAL ANALYSIS; PROTEIN DOMAIN; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CELL MEMBRANE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PLATELET GLYCOPROTEIN GPIIB-IIIA COMPLEX; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION;

EID: 64749101260     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2009.02.022     Document Type: Article

References (40)

1. Adair B.D., and Yeager M. Three-dimensional model of the human platelet integrin αIIbß3 based on electron cryomicroscopy and x-ray crystallography. Proc. Natl. Acad. Sci. USA 99 (2002) 14059-14064
2. Barth P., Schonbrun J., and Baker D. Toward high-resolution prediction and design of transmembrane helical protein structures. Proc. Natl. Acad. Sci. USA 104 (2007) 15682-15687
3. Barth P., Wallner B., and Baker D. Prediction of membrane protein structures with complex topologies using limited constraints. Proc. Natl. Acad. Sci. USA 106 (2009) 1409-1414
4. Bass R.B., Butler S.L., Chervitz S.A., Gloor S.L., and Falke J.J. Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis. Methods Enzymol. 423 (2007) 25-51
5. Bocharov E.V., Mayzel M.L., Volynsky P.E., Goncharuk M.V., Ermolyuk Y.S., Schulga A.A., Artemenko E.O., Efremov R.G., and Arseniev A.S. Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1. J. Biol. Chem. 283 (2008) 29385-29395
6. Bocharov E.V., Mineev K.S., Volynsky P.E., Ermolyuk Y.S., Tkach E.N., Sobol A.G., Chupin V.V., Kirpichnikov M.P., Efremov R.G., and Arseniev A.S. Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state. J. Biol. Chem. 283 (2008) 6950-6956
7. Brunger A.T., Clore G.M., Gronenborn A.M., Saffrich R., and Nilges M. Assessing the quality of solution nuclear magnetic resonance structures by complete cross-validation. Science 261 (1993) 328-331
8. Call M.E., Schnell J.R., Xu C., Lutz R.A., Chou J.J., and Wucherpfennig K.W. The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor. Cell 127 (2006) 355-368
9. Chothia C., Levitt M., and Richardson D. Helix to helix packing in proteins. J. Mol. Biol. 145 (1981) 215-250
10. Das R., and Baker D. Macromolecular modeling with rosetta. Annu. Rev. Biochem. 77 (2008) 363-382
11. Davis I.W., Leaver-Fay A., Chen V.B., Block J.N., Kapral G.J., Wang X., Murray L.W., Arendall III W.B., Snoeyink J., Richardson J.S., and Richardson D.C. MolProbity: All-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35 (2007) W375-W383
12. Duneau J.P., Vegh A.P., and Sturgis J.N. A dimerization hierarchy in the transmembrane domains of the HER receptor family. Biochemistry 46 (2007) 2010-2019
13. Gottschalk K.E. A coiled-coil structure of the αIIbß3 integrin transmembrane and cytoplasmic domains in its resting state. Structure 13 (2005) 703-712
14. Hughes P.E., Diaz-Gonzalez F., Leong L., Wu C., McDonald J.A., Shattil S.J., and Ginsberg M.H. Breaking the integrin hinge. J. Biol. Chem. 271 (1996) 6571-6574
15. Kovalenko O.V., Yang X., Kolesnikova T.V., and Hemler M.E. Evidence for specific tetraspanin homodimers: Inhibition of palmitoylation makes cysteine residues available for cross-linking. Biochem. J. 377 (2004) 407-417
16. Lau T.L., Dua V., and Ulmer T.S. Structure of the integrin alphaIIb transmembrane segment. J. Biol. Chem. 283 (2008) 16162-16168
17. Lau T.L., Partridge A.W., Ginsberg M.H., and Ulmer T.S. Structure of the integrin beta3 transmembrane segment in phospholipid bicelles and detergent micelles. Biochemistry 47 (2008) 4008-4016
18. Li R., Babu C.R., Lear J.D., Wand A.J., Bennett J.S., and Degrado W.F. Oligomerization of the integrin aIIbb3: Roles of the transmembrane and cytoplasmic domains. Proc. Natl. Acad. Sci. USA 98 (2001) 12462-12467
19. Li W., Metcalf D.G., Gorelik R., Li R., Mitra N., Nanda V., Law P.B., Lear J.D., Degrado W.F., and Bennett J.S. A push-pull mechanism for regulating integrin function. Proc. Natl. Acad. Sci. USA 102 (2005) 1424-1429
20. Liu W., Crocker E., Siminovitch D.J., and Smith S.O. Role of side-chain conformational entropy in transmembrane helix dimerization of glycophorin A. Biophys. J. 84 (2003) 1263-1271
21. Luo B.H., Springer T.A., and Takagi J. A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol. 2 (2004) e153
22. Luo B.H., Carman C.V., Takagi J., and Springer T.A. Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering. Proc. Natl. Acad. Sci. USA 102 (2005) 3679-3684
23. Luo B.H., Carman C.V., and Springer T.A. Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 25 (2007) 619-647
24. MacKenzie K.R., Prestegard J.H., and Engelman D.M. A transmembrane helix dimer: Structure and implications. Science 276 (1997) 131-133
25. McLaughlin S., Smith S.O., Hayman M.J., and Murray D. An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family. J. Gen. Physiol. 126 (2005) 41-53
26. Moser M., Nieswandt B., Ussar S., Pozgajova M., and Fassler R. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat. Med. 14 (2008) 325-330
27. O'Toole T.E., Katagiri Y., Faull R.J., Peter K., Tamura R., Quaranta V., Loftus J.C., Shattil S.J., and Ginsberg M.H. Integrin cytoplasmic domains mediate inside-out signal transduction. J. Cell Biol. 124 (1994) 1047-1059
28. Partridge A.W., Liu S., Kim S., Bowie J.U., and Ginsberg M.H. Transmembrane domain helix packing stabilizes integrin aIIbb3 in the low affinity state. J. Biol. Chem. 280 (2005) 7294-7300
29. Richardson J.S., and Richardson D.C. Principles and Patterns of Protein Conformation. In: Fasman G.D. (Ed). Prediction of Protein Structure and the Principles of Protein Conformation (1989), Plenum Press, New York 1-98
30. Smith S.O., Song D., Shekar S., Groesbeek M., Ziliox M., and Aimoto S. Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers. Biochemistry 40 (2001) 6553-6558
31. Ulmer T.S., Yaspan B., Ginsberg M.H., and Campbell I.D. NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb beta 3 in aqueous solution. Biochemistry 40 (2001) 7498-7508
32. 3 "inside-out" activation as regulated by its cytoplasmic face. Cell 110 (2002) 587-597
33. Vinogradova O., Vaynberg J., Kong X., Haas T.A., Plow E.F., and Qin J. Membrane-mediated structural transitions at the cytoplasmic face during integrin activation. Proc. Natl. Acad. Sci. USA 101 (2004) 4094-4099
34. von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225 (1992) 487-494
35. Wegener K.L., Partridge A.W., Han J., Pickford A.R., Liddington R.C., Ginsberg M.H., and Campbell I.D. Structural basis of integrin activation by talin. Cell 128 (2007) 171-182
36. Wegener K.L., and Campbell I.D. Transmembrane and cytoplasmic domains in integrin activation and protein-protein interactions. Mol. Membr. Biol. 25 (2008) 376-387
37. Weljie A.M., Hwang P.M., and Vogel H.J. Solution structures of the cytoplasmic tail complex from platelet αIIb- and β3-subunits. Proc. Natl. Acad. Sci. USA 99 (2002) 5878-5883
38. Xiong Y.M., Chen J., and Zhang L. Modulation of CD11b/CD18 adhesive activity by its extracellular, membrane-proximal regions. J. Immunol. 171 (2003) 1042-1050
39. Zhang X., Gureasko J., Shen K., Cole P.A., and Kuriyan J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125 (2006) 1137-1149
40. Zhu J., Luo B.H., Xiao T., Zhang C., Nishida N., and Springer T.A. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol. Cell 32 (2008) 849-861