title: Proposed structure of the A domains of factor VIII by homology modelling.
abstract: We have predicted a structure for the three A domains of blood coagulation factor VIII by virtue of their homology to blue copper-binding proteins. This structure, consisting of six beta-barrels, is arranged in a triangular configuration with a single type II copper-binding site linking the A1 and A3 domains.
authors.forename: Y
authors.initials: Y
authors.lastname: Pan
authors.forename: T
authors.initials: T
authors.lastname: DeFay
authors.forename: J
authors.initials: J
authors.lastname: Gitschier
authors.forename: F E
authors.initials: FE
authors.lastname: Cohen
mesh_terms: D000595:Amino Acid Sequence; D001204:Ascorbate Oxidase / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002570:Ceruloplasmin / Q000737:chemistry / Q000378:metabolism; D003300:Copper / Q000378:metabolism; D005169:Factor VIII / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D009572:Nitrite Reductases / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D003300:Copper; D005169:Factor VIII; D001204:Ascorbate Oxidase; D002570:Ceruloplasmin; D009572:Nitrite Reductases