Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain
作者： T. A. Springer
DOI: 10.1073/PNAS.94.1.65
关键词: Peptide sequence 、 Biochemistry 、 Protein structure 、 Binding site 、 G alpha subunit 、 Integrin 、 Stereochemistry 、 Protein folding 、 Phospholipase D 、 ATP synthase alpha/beta subunits 、 Biology
摘要: The N-terminal approximately 440 aa of integrin alpha subunits contain seven sequence repeats. These are predicted here to fold into a beta-propeller domain. A homologous domain from the enzyme phosphatidylinositol phospholipase D is have same fold. domains four-stranded beta-sheets arranged in torus around pseudosymmetry axis. trimeric G-protein beta subunit (G beta) appears be most closely related beta-propeller. Integrin ligands and putative Mg2+ ion bind upper face This binds substrates enzymes used by G protein subunit. I domain, which structurally subunit, tethered top hinge that may allow movement relative one another. Ca2+-binding motifs on lower
harvard.edu
sci-hub.se 参考文章(62)
F.M. Vellieux, F. Huitema, H. Groendijk, K.H. Kalk, J.F. Jzn, J.A. Jongejan, J.A. Duine, K. Petratos, J. Drenth, W.G. Hol, Structure of quinoprotein methylamine dehydrogenase at 2.25 A resolution. The EMBO Journal. ,vol. 8, pp. 2171- 2178 ,(1989) , 10.1002/J.1460-2075.1989.TB08339.X
D S Tuckwell, A Brass, M J Humphries, Homology modelling of integrin EF-hands. Evidence for widespread use of a conserved cation-binding site. Biochemical Journal. ,vol. 285, pp. 325- 331 ,(1992) , 10.1042/BJ2850325
J J Calvete, A Henschen, J González-Rodríguez, Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb. Biochemical Journal. ,vol. 261, pp. 561- 568 ,(1989) , 10.1042/BJ2610561
J C Loftus, J W Smith, M H Ginsberg, Integrin-mediated cell adhesion: the extracellular face. Journal of Biological Chemistry. ,vol. 269, pp. 25235- 25238 ,(1994) , 10.1016/S0021-9258(18)47235-3
Burkhard Rost, PHD: predicting one-dimensional protein structure by profile-based neural networks. Methods in Enzymology. ,vol. 266, pp. 525- 539 ,(1996) , 10.1016/S0076-6879(96)66033-9
J.W. Weisel, C Nagaswami, G Vilaire, J.S. Bennett, Examination of the platelet membrane glycoprotein IIb-IIIa complex and its interaction with fibrinogen and other ligands by electron microscopy. Journal of Biological Chemistry. ,vol. 267, pp. 16637- 16643 ,(1992) , 10.1016/S0021-9258(18)42050-9
S E D'Souza, M H Ginsberg, T A Burke, E F Plow, The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its alpha subunit. Journal of Biological Chemistry. ,vol. 265, pp. 3440- 3446 ,(1990) , 10.1016/S0021-9258(19)39787-X
Joseph C. Loftus, Carol E. Halloran, Mark H. Ginsberg, Larry P. Feigen, Jeffery A. Zablocki, Jeffrey W. Smith, The Amino-terminal One-third of αIIb Defines the Ligand Recognition Specificity of Integrin αIIbβ3(∗) Journal of Biological Chemistry. ,vol. 271, pp. 2033- 2039 ,(1996) , 10.1074/JBC.271.4.2033
J W Smith, D A Cheresh, Integrin (alpha v beta 3)-ligand interaction. Identification of a heterodimeric RGD binding site on the vitronectin receptor. Journal of Biological Chemistry. ,vol. 265, pp. 2168- 2172 ,(1990) , 10.1016/S0021-9258(19)39956-9
Cristina PUJADES, Joaquin TEIXIDÓ, Gianfranco BAZZONI, Martin E. HEMLER, Integrin alpha 4 cysteines 278 and 717 modulate VLA-4 ligand binding and also contribute to alpha 4/180 formation. Biochemical Journal. ,vol. 313, pp. 899- 908 ,(1996) , 10.1042/BJ3130899