title: S28 peptidases: lessons from a seemingly 'dysfunctional' family of two.
abstract: A recent paper in BMC Structural Biology reports the crystal structure of human prolylcarboxypeptidase (PRCP), one of the two members of the S28 peptidase family. Comparison of the substrate-binding site of PRCP with that of its family partner, dipeptidyl dipeptidase 7 (DPP7), helps to explain the different enzymatic activities of these structurally similar proteins, and also reveals a novel apparent charge-relay system in PRCP involving the active-site catalytic histidine. See research article: http://www.biomedcentral.com/1472-6807/10/16/
authors.affiliation: ActivX Biosciences, Inc, La Jolla, CA 92027, USA. johnk@activx.com
authors.forename: John W
authors.initials: JW
authors.lastname: Kozarich
mesh_terms: D002268:Carboxypeptidases / Q000235:genetics* / Q000378:metabolism; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D005810:Multigene Family / Q000235:genetics*; D011487:Protein Conformation; D013379:Substrate Specificity
chemical_list: D002268:Carboxypeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C100151:dipeptidyl peptidase II; C022448:lysosomal Pro-X carboxypeptidase