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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/

SUBMITTER: Kozarich JW

PROVIDER: S-EPMC2893137 | biostudies-literature | 2010

REPOSITORIES: biostudies-literature

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S28 peptidases: lessons from a seemingly 'dysfunctional' family of two.

Kozarich John W JW

BMC biology 20100628

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: ...[more]

PMID: 20598110

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