1IDO
I-DOMAIN FROM INTEGRIN CR3, MG2+ BOUND
Summary for 1IDO
Entry DOI | 10.2210/pdb1ido/pdb |
Descriptor | INTEGRIN, MAGNESIUM ION (3 entities in total) |
Functional Keywords | integrin, cell adhesion protein, glycoprotein, extracellular matrix, cytoskeleton |
Biological source | Homo sapiens (human) |
Cellular location | Cell membrane ; Single-pass type I membrane protein : P11215 |
Total number of polymer chains | 1 |
Total formula weight | 21687.01 |
Authors | Lee, J.-O.,Liddington, R. (deposition date: 1996-03-12, release date: 1996-08-01, Last modification date: 2024-02-07) |
Primary citation | Lee, 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: 7867070DOI: 10.1016/0092-8674(95)90517-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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