Ontology highlight
ABSTRACT:
SUBMITTER: Bah A
PROVIDER: S-EPMC2740429 | biostudies-literature | 2009 Jul
REPOSITORIES: biostudies-literature
Bah Alaji A Carrell Christopher J CJ Chen Zhiwei Z Gandhi Prafull S PS Di Cera Enrico E
The Journal of biological chemistry 20090527 30
Previous studies have shown that deletion of nine residues in the autolysis loop of thrombin produces a mutant with an anticoagulant propensity of potential clinical relevance, but the molecular origin of the effect has remained unresolved. The x-ray crystal structure of this mutant solved in the free form at 1.55 A resolution reveals an inactive conformation that is practically identical (root mean square deviation of 0.154 A) to the recently identified E* form. The side chain of Trp(215) colla ...[more]