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Functional mapping of the A2 domain from human factor VIII
J.-L. Plantier (1), D. Saboulard (2), J.-L. Pellequer (3), C. Négrier (1), M. Delcourt (2, 4)
(1) Laboratoire d’hémobiologie EA4174-IFR62 Faculté de médecine RTH Laennec, Université de Lyon, Lyon, France; (2) Biométhodes, Evry, France; (3) CEA, iBEB, Service de Biochimie et Toxicologie Nucléaire, Bagnols sur Cèze, France; (4) Present address: Global Bioenergies, Evry, France
Summary
Coagulation factor VIII (FVIII) is a multidomain glycoprotein in which the FVIII A2 domain is a key structural element. We aimed at identifying residues within FVIII A2 domain that are crucial for the maintenance of the cofactor function. A high number (n=206) of mutants were generated by substituting original residues with alanine. The mutants were expressed in COS-1 cells and their antigen levels and procoagulant activities were measured. The residues were classified in three categories: those with a non-detrimental alteration of their activities (activity >50 % of control FVIII; n=98), those with a moderate alteration (15 %
Keywords
factor VIII, Coagulation factors, protein function / activity, protein structure / folding
DOI
http://dx.doi.org/10.1160/TH11-07-0492You may also be interested in...
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