1v7p | pdb_00001v7p

Structure of EMS16-alpha2-I domain complex

spinqualitylabelsall models 1v7p, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1v7p is a 3 chain structure with sequence from Echis multisquamatus and Human. The February 2011 RCSB PDB Molecule of the Month feature on Integrin by David Goodsell is 10.2210/rcsb_pdb/mom_2011_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MN, NAG, PO4 Related: 1ukm, 1aox, 1dzi Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SLA_ECHML] EMS16 is a potent and selective inhibitor of alpha-2/beta-1 (ITGA2/ITGB1) integrin and acts as a potent antagonist of platelet aggregation and cell migration. Binds specifically to the I domain of the alpha-2 subunit, in a metal ion-independent fashion. [ITA2_HUMAN] Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix. [SLB_ECHML] EMS16 is a potent and selective inhibitor of alpha-2/beta-1 (ITGA2/ITGB1) integrin and acts as a potent antagonist of platelet aggregation and cell migration. Binds specifically to the I domain of the alpha-2 subunit, in a metal ion-independent fashion. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Snake venoms contain a number of heterodimeric C-type lectin-like proteins (CLPs) that interact specifically with components of the haemostatic system. EMS16 from the venom of Echis multisquamatus binds to the collagen receptor, integrin alpha2beta1, also known as glycoprotein (GP) Ia/IIa, and specifically inhibits collagen binding. Here we report the crystal structure of EMS16 in complex with recombinant integrin alpha2-I domain that plays a central role in collagen binding. The structure of the complex at 1.9 Angstrom resolution reveals that the collagen-binding site of the alpha2-I domain is covered completely by the bound EMS16. This blockage by EMS16 appears to spatially inhibit collagen binding to the alpha2-I domain. The bound alpha2-I domain adopts a closed conformation, which is seen in the absence of ligand, suggesting that EMS16 stabilizes a closed conformation corresponding to the less active structure of the alpha2-I domain. EMS16 does not directly bind to the manganese ion and residues of the metal ion-dependent adhesion site (MIDAS) of the alpha2-I domain, suggesting that EMS16 may have the potential to bind specifically to the alpha2-I domain in a metal ion-independent fashion. Crystal structure of EMS16 in complex with the integrin alpha2-I domain.,Horii K, Okuda D, Morita T, Mizuno H J Mol Biol. 2004 Aug 6;341(2):519-27. PMID:15276841 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Integrin 3D structures

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