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Article

Increasing hydrophobicity or disulfide bridging at the factor VIII A1 and C2 domain interface enhances procofactor stability.

The Journal of biological chemistry - 22 Jul 2011

Wakabayashi Hironao, Griffiths Amy E, Fay Philip J

Abstract excerpt

Factor VIII (FVIII) consists of a heavy (A1A2B domains) and light chain (A3C1C2 domains), whereas the contiguous A1A2 domains are separate subunits in the cofactor, FVIIIa. FVIII x-ray structures show close contacts between A1 and C2 domains. To explore the role of this region in FVIII(a) stability, we generated a variant containing a disulfide bond between A1 and C2 domains by mutating Arg-121 and Leu-2302 to...

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Identifiers

PMID: 21628455
DOI: 10.1074/jbc.M111.241109
PMCID: PMC3138256

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Increasing hydrophobicity or disulfide bridging at the factor VIII A1 and C2 domain interface enhances procofactor stability.PMID 21628455Read ↗

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