1oak
From Proteopedia
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CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 DOMAIN IN COMPLEX WITH THE FUNCTION BLOCKING NMC-4 FAB
Contents |
Overview
The presence of one or more copies of von Willebrand factor type A domains, identifies a superfamily of proteins usually involved in biological, processes controlled by specific molecular interactions, often adhesive in, nature. We have solved the crystal structure of the prototypic von, Willebrand factor A1 domain, essential for the antihemorrhagic activity of, platelets, in complex with the function blocking antibody, NMC-4, at 2.2 A, resolution. This has led to the recognition of a putative binding groove, for the platelet receptor, glycoprotein Ib alpha, formed by two adjacent, alpha-helices and a beta-strand. The structure also shows a contact, interface between A1 domain pairs, suggesting a hypothetical mechanism for, the regulation of protein assembly and heterologous ligand binding, mediated by homophilic interactions of type A domains.
Disease
Known diseases associated with this structure: von Willebrand disease OMIM:[193400]
About this Structure
1OAK is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab., Celikel R, Varughese KI, Madhusudan, Yoshioka A, Ware J, Ruggeri ZM, Nat Struct Biol. 1998 Mar;5(3):189-94. PMID:9501911
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