PMID: 11546839

 

    Legend: Gene, Sites

Title : Crystal structure of the extracellular segment of integrin alpha Vbeta3

Abstract :

1. Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands
2. We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3 .1 A resolution
3. Its 12 domains assemble into an ovoid "head" and two "tails.
4. 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
5. 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
6. A metal ion-dependent adhesion site ( MIDAS ) in the betaA domain is position ed to participate in a ligand-binding interface formed of loops from the propeller and betaA domains
7. MIDAS lies adjacent to a calcium-binding site with a potential regulatory function

Output (sent_index, trigger, protein, sugar, site):

Output(Part-Of) (sent_index, protein, site):

• 4. -, tails

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX
integrin alphaVbeta3 at 3	3685	2