Structures of the platelet calcium- and integrin-binding protein and the α(IIb)-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies

Journal of Molecular Recognition

Volumn 13, Issue 2, 2000, Pages 83-92

  Hwang, P M ^a   Vogel, H J ^a  

^a UNIVERSITY OF CALGARY   (Canada)

Author keywords

Calcineurin; Calcium; Calmodulin; Homology modelling; Integrin; NMR; Platelet

Indexed keywords

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; BINDING SITE; CALCINEURIN; CALCIUM BINDING PROTEIN; CALCIUM CELL LEVEL; CALMODULIN; CARBOXY TERMINAL SEQUENCE; INTEGRIN BINDING PROTEIN; MODEL; PROTEIN BINDING; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; BLOOD PLATELETS; CALCINEURIN; CALCIUM; CALCIUM-BINDING PROTEINS; CALMODULIN; CARRIER PROTEINS; CIRCULAR DICHROISM; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLATELET GLYCOPROTEIN GPIIB-IIIA COMPLEX; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0034060568     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1352(200003/04)13:2<83::AID-JMR491>3.0.CO;2-A     Document Type: Article

References (48)

1. Babu YS, Sacks JS, Greenhough TJ, Bugg CE, Means AR, Cook WJ. 1985. Three dimensional structure of calmodulin. Nature 315: 37-40.
2. 2+-binding protein, p22, is required for constitutive membrane traffic. J. Biol. Chem. 271: 10183-10187.
3. Brünger AT. 1992. X-PLOR (Version 3. V Manual. Yale University Press, New Haven, CT.
4. Burns K, Duggan B, Atkinson EA, Famulski KS, Nemer M, Bleackley RC, Michalak M. 1994. Modulation of gene expression by calreticulin binding to the glucocorticoid receptor. Nature 367: 476-480.
5. Burridge K, Faith K, Kelly T, Nuckolls G, Turner C. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. A. Rev. Cell. Biol. 4: 487-525.
6. Casari G, Sippl MJ. 1992. Structure-derived hydrophobic potential. J. Mol. Biol. 224: 725-732.
7. Chattopadhyaya R, Meador WE, Means AR, Quiocho FA. 1992. Calmodulin structure refined at 1.7 Å resolution. J. Mol. Biol. 228: 1177-1192.
8. Cook WJ, Jeffrey LC, Cox JA, Vijay-Kumar S. 1993. Structure of a sarcoplasmic calcium-binding protein from amphioxus refined at 2.4 Å resolution. J. Mol. Biol. 229: 461-471.
9. 1 with calreticulin. J. Biol. Chem. 270: 23132-23138.
10. Coppolino MG, Woodside MJ, Demaurex N, Grinstein S, St-Arnaud R, Dedhar S. 1997. Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion. Nature 386: 843-847.
11. Crivici A, Ikura M. 1995. Molecular and structural basis of target recognition by calmodulin. A. Rev. Biophys. Biomol. Struct. 24: 85-116.
12. Dedhar S, Hannigan GE. 1996. Integrin cytoplasmic interactions and bidirectional transmembrane signalling. Curr. Opin. Cell Biol. 8: 657-669.
13. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. 1995. NMRPIPE: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
14. 3. J. Biol Chem. 268: 23087-23092.
15. Flaherty KM, Zozulya S, Stryer L, McKay DB. 1993. Three-dimensional structure of recoverin, a calcium sensor in vision. Cell 75: 709-716.
16. 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J. Biol. Chem. 266: 17106-17111.
17. Griffith JP, Kim JL, Kim EE, Sintchak MD, Thomson JA, Fitzgibbon MJ, Fleming MA, Caron PR, Hsiao K, Navia MA. 1995. X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell 82: 507-522.
18. 3. A ternary complex of the integrin α and β subunits and a divalent cation. J. Biol. Chem. 271: 6017-6026.
19. Horwitz AF. 1997. Integrins and health. Sci Am. 278: 68-75.
20. Hughes PE, Diaz-Gonzalez F, Leong L, Wu C, McDonald JA, Shattil SJ, Ginsberg MH. 1996. Breaking the integrin hinge. J. Biol Chem. 271: 6571-6574.
21. Hynes RO. 1992. Integrins: versatility, modulation, and signalling in cell adhesion. Cell 69: 11-25.
22. Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showaiter RE, Moomaw EW, Gastinel LN, Habuka N, Chen X, Maldonado F, Barker JE, Bacquet R, Villafranca JE. 1995. Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature 378: 641-644.
23. Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. 1995. Solution structure of calcium-free calmodulin. Nature Struct. Biol. 2: 768-776.
24. Lin X, Barber DL. 1996. A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange. Proc. Natl Acad. Sci. USA 93: 12631-12636.
25. Meador WE, Means AR, Quiocho FA. 1992. Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science 257: 1251-1255.
26. Meador WE, Means AR, Quiocho FA. 1993. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262: 1718-1721.
27. Milan D, Griffith J, Su M, Price ER, McKeon F. 1994. The latch region of calcineurin B is involved in both immunosuppressant-immunophilin complex docking and phosphatase activation. Cell 79: 437-447.
28. IIb cytoplasmic domain. J. Biol. Chem. 272: 4651-4654.
29. Nash PD, Opas M, Michalak M. 1994. Calreticulin: not just another calcium-binding protein. Mol. Cell. Biochem. 135: 71-78.
30. IIb. Science 254: 845-847.
31. O'Toole TE, Katagiri Y, Faull RJ, Karlheinz P, Tamura R, Quaranta V, Loftus JC, Shattil SJ, Ginsberg MH. 1994. Integrin cytoplasmic domains mediate inside-out signal transduction. J. Cell Biol. 124: 1047-1059.
32. Poncz M, Eisman R, Heidenreich R, Silver SM, Viliaire G, Surrey S, Schwartz E, Bennett JS. 1987. Structure of platelet membrane glycoprotein IIb. J. Biol. Chem. 262: 8476-8482.
33. Shock DD, Naik UP, Brittain JE, Alahari SK, Sondek J, Parise LV. 1999. Calcium-dependent properties of CIB binding to the integrin αIIb cytoplasmic domain and translocation to the platelet cytoskeleton. Biochem. J. 342: 729-735.
34. Sims PJ, Ginsberg MH, Plow EF, Shattil SJ. 1991. Effect of platelet activation on the conformation of the plasma membrane glycoprotein IIb-IIIa complex. J. Biol. Chem. 266: 7345-7352.
35. Sippl MJ, Weitckus S. 1992. Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a data base of known protein conformations. Proteins 13: 258-271.
36. Stemmer PM, Klee CB. 1994. Dual calcium ion regulation of calcineurin by calmodulin and calcineurin B. Biochemistry 33: 6859-6866.
37. IIb cytoplasmic tail binding to β3 and to calcium- and integrin-binding protein. J. Biol. Chem. 274: 17257-17266.
38. Vijay-Kumar S, Cook WJ. 1992. Structure of a sarcoplasmic calcium-binding protein from Neireis diversicolor refined at 2.0 Å resolution. J. Mol. Biol. 224: 413-426.
39. Vogel HJ. Calmodulin: a versatile calcium mediator protein. 1994. Biochem. Cell Biol. 72: 357-376.
40. Vogel HJ, Zhang M. 1995. Protein engineering and NMR studies of calmodulin. Mol. Cell. Biochem. 149-150: 3-15.
41. Weisel JW, Nagaswami C, Viliaire G, Bennett JS. 1992. Examination of the platelet membrane glycoprotein IIb-IIIa complex and its interaction with fibrinogen and other ligands by electron microscopy. J. Biol. Chem. 267: 16637-16643.
42. Williams MJ, Hughes PE, O'Toole TE, Ginsberg MH. 1994. The inner world of cell adhesion: integrin cytoplasmic domains. Trends Cell Biol. 4: 109-112.
43. Wishart DS, Sykes BD. 1994. Chemical shifts as a tool for structure determination. Meth. Enzymol. 239: 363-392.
44. Wüthrich K. 1986. NMR of Proteins and Nucleic Acids. J Wiley, New York.
45. Wüthrich K, Billeter M, Braun W. 1983. Pseudostructures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169: 949-961.
46. Yamada KM, Miyamoto S. 1995. Integrin transmembrane signalling and cytoskeletal control. Curr. Opin. Cell Biol. 7: 681-689.
47. Zhang M, Yuan T, Vogel HJ. 1993. A peptide analog of the calmodulin-binding domain of myosin light chain kinase adopts an alpha-helical structure in aqueous trifluoroethanol. Protein Sci. 2: 1931-1937.
48. Zhang M, Tanaka T, Ikura M. 1995. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Struct. Biol. 2: 758-767.