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- Title
Crystal structure of the extracellular segment of integrin alpha Vbeta3.
- Authors
Xiong, J P; Stehle, T; Diefenbach, B; Zhang, R; Dunker, R; Scott, D L; Joachimiak, A; Goodman, S L; Arnaout, M A
- Abstract
Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands. We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution. Its 12 domains assemble into an ovoid "head" and two "tails." In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation. The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins. A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains. MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.
- Publication
Science (New York, N.Y.), 2001, Vol 294, Issue 5541, p339
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.1064535