title: Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains.
abstract: Coagulation factors IX/X-binding protein is an intertwined dimer with a central loop projecting into the adjoining subunit. Excluding this loop, each subunit has a fold similar to rat mannose-binding protein.
authors.forename: H
authors.initials: H
authors.lastname: Mizuno
authors.forename: Z
authors.initials: Z
authors.lastname: Fujimoto
authors.forename: M
authors.initials: M
authors.lastname: Koizumi
authors.forename: H
authors.initials: H
authors.lastname: Kano
authors.forename: H
authors.initials: H
authors.lastname: Atoda
authors.forename: T
authors.initials: T
authors.lastname: Morita
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D003435:Crotalid Venoms; D018360:Crystallography, X-Ray; D019281:Dimerization; D037241:Mannose-Binding Lectins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D051381:Rats; D030162:Reptilian Proteins; D017386:Sequence Homology, Amino Acid
chemical_list: D002352:Carrier Proteins; D003435:Crotalid Venoms; D037241:Mannose-Binding Lectins; D030162:Reptilian Proteins; C070302:factor IX-factor X-binding protein, Crotalinae