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Sci. STKE, 16 October 2001
Vol. 2001, Issue 104, p. tw386
[DOI: 10.1126/stke.2001.104.tw386]

EDITORS' CHOICE

ADHESION Only Connect

Abstract: Integrins are large, heterodimeric ({alpha}ß) transmembrane proteins that bind to many extracellular components as well as to other cell adhesion proteins. They are important in normal cellular processes, such as attachment, migration, and proliferation, and are also implicated in pathological states such as neoplasia and metastasis. Xiong et al. (Perspective by Humphries and Mould) present the crystal structure of the extracellular regions of the complex of {alpha}V and ß3. There are 12 domains, of which the most interesting are the amino-terminal propeller from the {alpha} chain and the A domain from the ß chain. This pair of domains forms an interface with similarity to that between the {alpha} and ß subunits of guanine nucleotide binding, or G proteins, and also contains the binding site for the Arg-Gly-Asp tripeptide motif present in many integrin ligands, such as fibronectin.

J.-P. Xiong, T. Stehle, B. Diefenbach, R. Zhang, R. Dunker, D. L. Scott, A. Joachimiak, S. L. Goodman, M. A. Arnaout, Crystal structure of the extracellular segment of integrin {alpha}Vß3. Science 294, 339-345 (2001). [Abstract] [Full Text]

M. J. Humphries, A. P. Mould, An anthropomorphic integrin. Science 294, 316-317 (2001). [Summary] [Full Text]

Citation: Only Connect. Sci. STKE 2001, tw386 (2001).

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Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)