CRYSTAL-STRUCTURE OF THE A-DOMAIN FROM THE A-SUBUNIT OF INTEGRIN CR3 (CD11B/CD18)

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We have determined the high resolution crystal structure of the A domain from the a chain of integrin CR3. The domain adopts a classic alpha/beta ''Rossmann'' fold and contains an unusual Mg2+ coordination site at its surface. One of the coordinating ligands is the glutamate side chain from another A domain molecule. We suggest that this site represents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands. We further propose that the beta subunits of integrins contain a MIDAS motif within a modified A domain. Our crystal structure will allow reliable models to be built for other members of the A domain superfamily and should facilitate development of novel adhesion modulatory drugs.
Publisher
CELL PRESS
Issue Date
1995
Language
English
Article Type
Article
Keywords

AMINO-ACID-SEQUENCE; BETA-SUBUNIT; VONWILLEBRAND-FACTOR; EXTRACELLULAR-MATRIX; ADHESION RECEPTOR; ALPHA-SUBUNIT; MONOCLONAL-ANTIBODIES; FIBRONECTIN RECEPTOR; MOLECULAR-CLONING; GLOBULAR DOMAINS

Citation

CELL, v.80, no.4, pp.631 - 638

ISSN
0092-8674
DOI
10.1016/0092-8674(95)90517-0
URI
http://hdl.handle.net/10203/71006
Appears in Collection
CH-Journal Papers(저널논문)
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