Article
Mutation of the surface-exposed amino acid Trp to Ala in the FVIII C2 domain results in defective secretion of the otherwise functional protein.
British journal of haematology - 1 Jun 2004
Schatz Simone M, Zimmermann Klaus, Hasslacher Meinhard, Kerschbaumer Randolf, Dockal Michael, Gritsch Herbert, Turecek Peter L, Schwarz Hans P, Dorner Friedrich, Scheiflinger Friedrich
Abstract excerpt
The C2 domain of factor VIII (FVIII) is important for FVIII-phospholipid (PL) and FVIII-von Willebrand factor (VWF) interactions. A FVIII structural model, derived by electron crystallography, suggests four hydrophobic loops at the FVIII C2 domain-PL interface. Within loop four, the solvent-exposed amino acid, Trp(2313), is believed to contribute to FVIII-PL binding. To analyse this interaction, the amino-acid...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
