Ontology highlight
ABSTRACT:
SUBMITTER: Papaconstantinou ME
PROVIDER: S-EPMC2667268 | biostudies-literature | 2008 Jun
REPOSITORIES: biostudies-literature
Papaconstantinou M E ME Bah A A Di Cera E E
Cellular and molecular life sciences : CMLS 20080601 12
The A chain of thrombin is covalently linked to the catalytic B chain but is separate from any known epitope for substrate recognition. In this study we present the results of the Ala replacement of 12 charged residues controlling the stability of the A chain and its interaction with the B chain. Residues Arg4 and Glu8 play a significant role in substrate recognition, even though they are located > 20 A away from residues of the catalytic triad, the primary specificity pocket and the Na+ site. T ...[more]