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1IDO

I-DOMAIN FROM INTEGRIN CR3, MG2+ BOUND

Summary for 1IDO
Entry DOI10.2210/pdb1ido/pdb
DescriptorINTEGRIN, MAGNESIUM ION (3 entities in total)
Functional Keywordsintegrin, cell adhesion protein, glycoprotein, extracellular matrix, cytoskeleton
Biological sourceHomo sapiens (human)
Cellular locationCell membrane ; Single-pass type I membrane protein : P11215
Total number of polymer chains1
Total formula weight21687.01
Authors
Lee, J.-O.,Liddington, R. (deposition date: 1996-03-12, release date: 1996-08-01, Last modification date: 2024-02-07)
Primary citationLee, J.O.,Rieu, P.,Arnaout, M.A.,Liddington, R.
Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18).
Cell(Cambridge,Mass.), 80:631-638, 1995
Cited by
PubMed Abstract: We have determined the high resolution crystal structure of the A domain from the alpha 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.
PubMed: 7867070
DOI: 10.1016/0092-8674(95)90517-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

227111

数据于2024-11-06公开中

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