1ohe

From Proteopedia

Revision as of 14:34, 15 February 2008

STRUCTURE OF CDC14B PHOSPHATASE WITH A PEPTIDE LIGAND

Overview

The Cdc14 family of dual-specificity protein phosphatases (DSPs) is, conserved within eukaryotes and functions to down-regulate mitotic Cdk, activities, promoting cytokinesis and mitotic exit. We have integrated, structural and kinetic analyses to define the molecular mechanism of the, dephosphorylation reaction catalysed by Cdc14. The structure of Cdc14, illustrates a novel arrangement of two domains, each with a DSP-like fold, arranged in tandem. The C-terminal domain contains the conserved PTP motif, of the catalytic site, whereas the N-terminal domain, which shares no, sequence similarity with other DSPs, contributes to substrate specificity, and lacks catalytic activity. The catalytic site is located at the base of, a pronounced surface channel formed by the interface of the two domains, and regions of both domains interact with the phosphopeptide substrate., Specificity for a pSer-Pro motif is mediated by a hydrophobic pocket that, is capable of accommodating the apolar Pro(P+1) residue of the peptide., Our structural and kinetic data support a role for Cdc14 in the, preferential dephosphorylation of proteins modified by proline-directed, kinases.

About this Structure

1OHE is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase., Gray CH, Good VM, Tonks NK, Barford D, EMBO J. 2003 Jul 15;22(14):3524-35. PMID:12853468

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