1ohd: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
==Overview== | ==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 ... | 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== | ==About this Structure== | ||
1OHD is a | 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]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OHD OCA]. | ||
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: protein phosphatase]] | [[Category: protein phosphatase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:14:54 2007'' | ||
