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Comparative molecular modeling of the active subunit of human kininase I
D Hendriks1, M Vingron, G Vriend
1Department of Pharmaceutical Sciences, University of Antwerp, Wilrijk, Belgium.
Abstract:
The structure of the enzymatically active subunit of human plasma carboxypeptidase N was determined by computer aided model building by homology using the structural coordinates from carboxypeptidase A. The active site of carboxypeptidase N has been well conserved in comparison with carboxypeptidase A. Differences in substrate specificity can be explained by the comparison of energetically favorable binding sites for different atomic probe groups.