Article
Protease and EGF1 domains of factor IXa play distinct roles in binding to factor VIIIa. Importance of helix 330 (helix 162 in chymotrypsin) of protease domain of factor IXa in its interaction with factor VIIIa.
The Journal of biological chemistry - 25 Jun 1999
Mathur A, Bajaj S P
Abstract excerpt
Previous studies revealed that cleavage at Arg-318-Ser-319 in the protease domain autolysis loop of factor IXa results in its diminished binding to factor VIIIa. Now, we have investigated the importance of adjacent surface-exposed helix 330-338 (162-170 in chymotrypsin numbering) of IXa in its interaction with VIIIa. IXWT, eight point mutants mostly based on hemophilia B patients, and a replacement mutant...
Topics
- Binding Sites
- Chymotrypsin
- Electrophoresis, Polyacrylamide Gel
- Factor IX
- Factor IXa
- Factor VIIIa
- Humans
- Models, Molecular
- Mutation
- Protein Binding
- Protein Conformation
- Protein Structure, Secondary
- Structure-Activity Relationship