1jv2
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CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Glanzmann thrombasthenia, type B OMIM:[173470]
About this StructureAbout this Structure
1JV2 is a Protein complex structure of sequences from Homo sapiens with NAG and CA as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the extracellular segment of integrin alpha Vbeta3., Xiong JP, Stehle T, Diefenbach B, Zhang R, Dunker R, Scott DL, Joachimiak A, Goodman SL, Arnaout MA, Science. 2001 Oct 12;294(5541):339-45. Epub 2001 Sep 6. PMID:11546839
Page seeded by OCA on Mon Nov 12 17:44:45 2007