title: Comparative molecular modeling of the active subunit of human kininase I.
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.
authors: Department of Pharmaceutical Sciences, University of Antwerp, Wilrijk, Belgium.
authors: D
authors: D
authors: Hendriks
authors: M
authors: M
authors: Vingron
authors: G
authors: G
authors: Vriend
authors: W
authors: W
authors: Wang
authors: D
authors: D
authors: Nalis
authors: S
authors: S
authors: Scharpé
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002268:Carboxypeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D043422:Carboxypeptidases A; D006801:Humans; D001121:Lysine Carboxypeptidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013379:Substrate Specificity; D013816:Thermodynamics
chemical_list: D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D001121:Lysine Carboxypeptidase