Correlation of factor IXa subsite modulations with effects on substrate discrimination.

ABSTRACT:

Background

A key feature of factor IXa is its allosteric transformation from an enzymatically latent form into a potent procoagulant. Although several small molecules have been found to be capable of partially affecting FIXa function (i.e. ethylene glycol, Ca(2+), and low molecular weight heparin [LMWH]), the resulting modest changes in peptidolytic activity have made the study of their mechanisms of action challenging. As these effects provide hints about potential regulatory forces that may be operational in the full expression of FIXa coagulant activity, their description remains of great interest. Studies of crystal structures have yielded insights into the structural changes induced by these effectors, but there remains a paucity of information to correlate any given structura

SUBMITTER: Neuenschwander PF 

PROVIDER: S-EPMC3291813 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature