1OAK

CRYSTAL STRUCTURE OF THE VON WILLEBRAND FACTOR (VWF) A1 DOMAIN IN COMPLEX WITH THE FUNCTION BLOCKING NMC-4 FAB

1OAK の概要

• エントリーDOI: 10.2210/pdb1oak/pdb
• 分子名称: NMC-4 IGG1, VON WILLEBRAND FACTOR, ... (4 entities in total)
• 機能のキーワード: von willebrand factor, glycoprotein iba (a:alpha) binding, complex (willebrand-immunoglobulin), blood coagulation, complex (willebrand-immunoglobulin) complex, complex (willebrand/immunoglobulin)
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Secreted: P04275
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 69793.49

構造登録者

Celikel, R.,Varughese, K.I. (登録日: 1997-12-18, 公開日: 1998-10-21, 最終更新日: 2024-11-20)

主引用文献

Celikel, R.,Varughese, K.I.,Madhusudan,Yoshioka, A.,Ware, J.,Ruggeri, Z.M.
Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab.
Nat.Struct.Biol., 5:189-194, 1998

PubMed Abstract: 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.

PubMed: 9501911
DOI: 10.1038/nsb0398-189

実験手法

X-RAY DIFFRACTION (2.2 Å)