1ohc
From Proteopedia
(New page: 200px<br /> <applet load="1ohc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ohc, resolution 2.50Å" /> '''STRUCTURE OF THE PR...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ohc. | + | [[Image:1ohc.jpg|left|200px]]<br /><applet load="1ohc" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ohc" size=" | + | |
caption="1ohc, resolution 2.50Å" /> | caption="1ohc, resolution 2.50Å" /> | ||
'''STRUCTURE OF THE PROLINE DIRECTED PHOSPHATASE CDC14'''<br /> | '''STRUCTURE OF THE PROLINE DIRECTED PHOSPHATASE CDC14'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1OHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1OHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHC OCA]. |
==Reference== | ==Reference== | ||
| Line 21: | Line 20: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:34:12 2008'' |
Revision as of 14:34, 15 February 2008
|
STRUCTURE OF THE PROLINE DIRECTED PHOSPHATASE CDC14
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
1OHC is a Single protein structure of sequence from Homo sapiens. 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
Page seeded by OCA on Fri Feb 15 16:34:12 2008
