Title : The Na+ binding channel of human coagulation proteases: novel insights on the structure and allosteric modulation revealed by molecular surface analysis.

Pub. Date : 2006 Feb 1

PMID : 16288954






2 Functional Relationships(s)
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1 We have characterized the structure, topography and lipophilicity of this channel in the ligand-free fast (sodium-bound) and slow (sodium-free) forms of thrombin, in the sole available structure of activated protein C and in several structures of the coagulation factors VIIa, IXa and Xa, differing in the nature of the bound inhibitor and in the occupancy of exosite-I as well as the Ca2+ and Na+ binding sites. Sodium coagulation factor II, thrombin Homo sapiens
2 We also disclosed major topographical changes on the thrombin"s surface upon sodium release and transition to the slow form that culminate in the narrowing of the S1 subsite entrance and, strikingly, in the loss of communication between the primary specificity pocket and the exosite-I. Sodium coagulation factor II, thrombin Homo sapiens