Crystal structure of the extracellular segment of integrin alpha Vbeta3.
Science
; 294(5541): 339-45, 2001 Oct 12.
Article
in En
| MEDLINE
| ID: mdl-11546839
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Receptors, Vitronectin
Type of study:
Prognostic_studies
Limits:
Humans
Language:
En
Journal:
Science
Year:
2001
Document type:
Article
Affiliation country:
Estados Unidos