1JV2

CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3

Summary for 1JV2

• Entry DOI: 10.2210/pdb1jv2/pdb
• Descriptor: INTEGRIN, ALPHA V, PLATELET MEMBRANE GLYCOPROTEIN IIIA BETA SUBUNIT, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: genu, hybrid domain, beta-tail domain, psi domain, egf domain, midas, admidas, cage motif, propeller, a-domain, thigh domain, calf domain, cell adhesion
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 186626.58

Authors

Xiong, J.P.,Stehle, T.,Diefenbach, B.,Zhang, R.,Dunker, R.,Scott, D.,Joachimiak, A.,Goodman, S.L.,Arnaout, M.A. (deposition date: 2001-08-28, release date: 2001-10-17, Last modification date: 2024-10-09)

Primary citation

Xiong, J.P.,Stehle, T.,Diefenbach, B.,Zhang, R.,Dunker, R.,Scott, D.L.,Joachimiak, A.,Goodman, S.L.,Arnaout, M.A.
Crystal structure of the extracellular segment of integrin alpha Vbeta3.
Science, 294:339-345, 2001

PubMed 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.

PubMed: 11546839
DOI: 10.1126/science.1064535

Experimental method

X-RAY DIFFRACTION (3.1 Å)