The solution structure of human coagulation factor VIIa in its complex with tissue factor is similar to free factor VIIa: a study of a heterodimeric receptor-ligand complex by X-ray and neutron scattering and computational modeling.

Ashton, A W; Boehm, M K; Johnson, D J; Kemball-Cook, G; Perkins, S J

Ashton, A W; Boehm, M K; Johnson, D J; Kemball-Cook, G; Perkins, S J.

Affiliation

Ashton AW; Department of Biochemistry and Molecular Biology, Royal Free Hospital School of Medicine, London, U. K.

Biochemistry ; 37(22): 8208-17, 1998 Jun 02.

Article in En | MEDLINE | ID: mdl-9609717

Subject(s)

Computer Simulation; Factor VIIa/chemistry; Models, Molecular; Thromboplastin/chemistry; Amino Acid Sequence; Animals; Cattle; Crystallization; Dimerization; Factor VIIa/metabolism; Humans; Ligands; Molecular Sequence Data; Neutrons; Protein Structure, Tertiary; Receptors, Cell Surface/chemistry; Receptors, Cell Surface/metabolism; Scattering, Radiation; Solutions; Swine; Thromboplastin/metabolism; Ultracentrifugation; X-Rays

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Collection: 01-internacional Database: MEDLINE Main subject: Computer Simulation / Thromboplastin / Models, Molecular / Factor VIIa Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: Biochemistry Year: 1998 Document type: Article Country of publication: United States

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