Crystal structure of the extracellular segment of integrin {alpha}V{beta}3.
Integrins are {alpha}{beta} 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 {alpha}V{sup {beta}}3 at 3.1 Angstroms resolution. Its 12 domains assemble into an ovoid 'head' and two 'tails.' In the crystal, {alpha}V{sup {beta}}3 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 {alpha}V and an A domain from {beta}3, and bears a striking resemblance to the G{alpha} /G{sup {beta}} interface in G proteins. A metal ion-dependent adhesion site (MIDAS) in the {beta}A domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and {beta}A domains. MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- USDOE; National Institutes of Health (NIH)
- DOE Contract Number:
- DE-AC02-06CH11357
- OSTI ID:
- 949403
- Report Number(s):
- ANL/BIO/JA-40631; SCEHDK; TRN: US201012%%199
- Journal Information:
- Science, Vol. 294, Issue 5541 ; OCt. 12, 2001; ISSN 0193-4511
- Country of Publication:
- United States
- Language:
- ENGLISH
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