1AO3
A3 DOMAIN OF VON WILLEBRAND FACTOR
Summary for 1AO3
| Entry DOI | 10.2210/pdb1ao3/pdb |
| Descriptor | VON WILLEBRAND FACTOR (2 entities in total) |
| Functional Keywords | collagen-binding, von willebrand, cell adhesion |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 39899.62 |
| Authors | Bienkowski, J.,Cruz, M.,Handin, R.,Liddington, R. (deposition date: 1997-07-16, release date: 1998-07-22, Last modification date: 2024-10-09) |
| Primary citation | Bienkowska, J.,Cruz, M.,Atiemo, A.,Handin, R.,Liddington, R. The von willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif. J.Biol.Chem., 272:25162-25167, 1997 Cited by PubMed Abstract: von Willebrand factor (vWF) is a multimeric plasma protein that mediates platelet adhesion to exposed subendothelium at sites of vascular injury. The A3 domain of vWF (vWF-A3) forms the principal binding site for collagens type I and III. We report here the crystal structure of the vWF-A3 domain at 2.2-A resolution. As expected, the structure is similar to the integrin I domain but with several novel features. Sequence alignments had suggested that the domain contained an integrin metal ion-dependent adhesion site (MIDAS) motif, but the crystal structure shows that the motif is modified and that no metal ion is bound. We have introduced mutations into the vestigial MIDAS motif and report that, unlike the I domain of integrin alpha2beta1, vWF-A3 continues to bind collagen after disruption of the motif. We conclude that collagen recognition by vWF-A3 occurs by a mechanism different from that of the integrin alpha2beta1. PubMed: 9312128DOI: 10.1074/jbc.272.40.25162 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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