Title : Molecular mapping of the thrombin-heparin cofactor II complex.

Pub. Date : 2004 Oct 8

PMID : 15292227






3 Functional Relationships(s)
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1 Four mutants (Asp51, Lys52, Lys145/Thr147/Trp148, Asp234) showed normal increased rates of inhibition by HCII-glycosaminoglycans, whereas four mutants (Trp50, Glu202, Glu229, Arg233) remained resistant to inhibition by HCII with glycosaminoglycans. Glycosaminoglycans serpin family D member 1 Homo sapiens
2 Collectively, our results support a "double bridge" mechanism for HCII inhibition of thrombin in the presence of glycosaminoglycans, which relies in part on ternary complex formation but is primarily dominated by an allosteric process involving contact of the "hirudin-like" domain of HCII with thrombin exosite-1. Glycosaminoglycans serpin family D member 1 Homo sapiens
3 Collectively, our results support a "double bridge" mechanism for HCII inhibition of thrombin in the presence of glycosaminoglycans, which relies in part on ternary complex formation but is primarily dominated by an allosteric process involving contact of the "hirudin-like" domain of HCII with thrombin exosite-1. Glycosaminoglycans serpin family D member 1 Homo sapiens