Title : Structural resiliency of an EGF-like subdomain bound to its target protein, thrombin.

Pub. Date : 1996 Feb

PMID : 8745396






4 Functional Relationships(s)
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1 Docking experiments revealed that the key contacts with thrombin are hydrophobic interactions between the side chains of residues Ile 414 and Ile 424 of thrombomodulin and a hydrophobic pocket on the thrombin surface. Isoleucine coagulation factor II, thrombin Homo sapiens
2 Docking experiments revealed that the key contacts with thrombin are hydrophobic interactions between the side chains of residues Ile 414 and Ile 424 of thrombomodulin and a hydrophobic pocket on the thrombin surface. Isoleucine coagulation factor II, thrombin Homo sapiens
3 Docking experiments revealed that the key contacts with thrombin are hydrophobic interactions between the side chains of residues Ile 414 and Ile 424 of thrombomodulin and a hydrophobic pocket on the thrombin surface. Isoleucine coagulation factor II, thrombin Homo sapiens
4 Residues Leu 415, Phe 419, and Ile 420, which would have been buried in intact EGF-like domains, are unfavorably exposed in the complex of thrombin with the EGF-like thrombomodulin fragment, thus providing a rationale for the enhancement of binding affinity upon the deletion of Ile 420. Isoleucine coagulation factor II, thrombin Homo sapiens