Secondary Substrate-binding Exosite in the Serine Protease Domain of Activated Protein C Important for Cleavage at Arg-506 but Not at Arg-306 in Factor Va
Open Access
- 1 June 2001
- journal article
- Published by Elsevier
- Vol. 276 (25) , 23105-23108
- https://doi.org/10.1074/jbc.m103138200
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Tracking Structural Features Leading to Resistance of Activated Protein C to α1-antitrypsinBiochemistry, 2000
- Structural investigation of the A domains of human blood coagulation factor V by molecular modelingProtein Science, 1998
- The effect of Arg306 → Ala and Arg506 → Gln substitutions in the inactivation of recombinant human factor Va by activated protein C and protein SProtein Science, 1997
- Binding sites for blood coagulation factor Xa and protein S involving residues 493–506 in factor VaProtein Science, 1996
- Mutation of Protease Domain Residues Lys37-39 in Human Protein C Inhibits Activation by the Thrombomodulin-Thrombin Complex without Affecting Activation by Free ThrombinJournal of Biological Chemistry, 1996
- Peptide Bond Cleavages and Loss of Functional Activity during Inactivation of Factor Va and Factor VaR506Q by Activated Protein CPublished by Elsevier ,1995
- Interactions and inhibition of blood coagulation factor Va involving residues 311–325 of activated protein CProtein Science, 1993
- The coagulation cascade: initiation, maintenance, and regulationBiochemistry, 1991
- The molecular basis of blood coagulationCell, 1988
- [6] Statistical analysis of enzyme kinetic dataPublished by Elsevier ,1979