1ohd
From Proteopedia
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| - | [[Image:1ohd.jpg|left|200px]]<br /><applet load="1ohd" size=" | + | [[Image:1ohd.jpg|left|200px]]<br /><applet load="1ohd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ohd, resolution 2.60Å" /> | caption="1ohd, resolution 2.60Å" /> | ||
'''STRUCTURE OF CDC14 IN COMPLEX WITH TUNGSTATE'''<br /> | '''STRUCTURE OF CDC14 IN COMPLEX WITH TUNGSTATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with WO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Wo4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1OHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=WO4:'>WO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Wo4+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein phosphatase]] | [[Category: protein phosphatase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:58:11 2008'' |
Revision as of 07:58, 3 February 2008
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STRUCTURE OF CDC14 IN COMPLEX WITH TUNGSTATE
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
1OHD is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Site: . 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 Sun Feb 3 09:58:11 2008
Categories: Homo sapiens | Single protein | Barford, D. | Good, V. | Gray, C. | Tonks, N. | WO4 | Cell cycle | Hydrolase | Protein phosphatase
