1c25
From Proteopedia
(Difference between revisions)
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<StructureSection load='1c25' size='340' side='right'caption='[[1c25]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1c25' size='340' side='right'caption='[[1c25]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1c25]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C25 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1c25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C25 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c25 OCA], [https://pdbe.org/1c25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c25 RCSB], [https://www.ebi.ac.uk/pdbsum/1c25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c25 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c25 OCA], [https://pdbe.org/1c25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c25 RCSB], [https://www.ebi.ac.uk/pdbsum/1c25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c25 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/MPIP1_HUMAN MPIP1_HUMAN] Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c25 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c25 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cdc25 phosphatases activate the cell division kinases throughout the cell cycle. The 2.3 A structure of the human Cdc25A catalytic domain reveals a small alpha/beta domain with a fold unlike previously described phosphatase structures but identical to rhodanese, a sulfur-transfer protein. Only the active-site loop, containing the Cys-(X)5-Arg motif, shows similarity to the tyrosine phosphatases. In some crystals, the catalytic Cys-430 forms a disulfide bond with the invariant Cys-384, suggesting that Cdc25 may be self-inhibited during oxidative stress. Asp-383, previously proposed to be the general acid, instead serves a structural role, forming a conserved buried salt-bridge. We propose that Glu-431 may act as a general acid. Structure-based alignments suggest that the noncatalytic domain of the MAP kinase phosphatases will share this topology, as will ACR2, a eukaryotic arsenical resistance protein. | ||
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| - | Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A.,Fauman EB, Cogswell JP, Lovejoy B, Rocque WJ, Holmes W, Montana VG, Piwnica-Worms H, Rink MJ, Saper MA Cell. 1998 May 15;93(4):617-25. PMID:9604936<ref>PMID:9604936</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1c25" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Cogswell JP]] | |
| - | [[Category: Cogswell | + | [[Category: Fauman EB]] |
| - | [[Category: Fauman | + | [[Category: Holmes W]] |
| - | [[Category: Holmes | + | [[Category: Lovejoy B]] |
| - | [[Category: Lovejoy | + | [[Category: Montana VG]] |
| - | [[Category: Montana | + | [[Category: Piwnica-Worms H]] |
| - | [[Category: Piwnica-Worms | + | [[Category: Rink MJ]] |
| - | [[Category: Rink | + | [[Category: Rocque WJ]] |
| - | [[Category: Rocque | + | [[Category: Saper MA]] |
| - | [[Category: Saper | + | |
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Current revision
HUMAN CDC25A CATALYTIC DOMAIN
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Categories: Homo sapiens | Large Structures | Cogswell JP | Fauman EB | Holmes W | Lovejoy B | Montana VG | Piwnica-Worms H | Rink MJ | Rocque WJ | Saper MA
