1c25

<StructureSection load='1c25' size='340' side='right' caption='[[1c25]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C25 FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c25 OCA], [http://pdbe.org/1c25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c25 RCSB], [http://www.ebi.ac.uk/pdbsum/1c25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c25 ProSAT]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c2/1c25_consurf.spt"</scriptWhenChecked>

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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1c25" style="background-color:#fffaf0;"></div>

*[[Tyrosine phosphatase|Tyrosine phosphatase]]

[[Category: Protein-tyrosine-phosphatase]]

[[Category: Cogswell, J P]]

[[Category: Fauman, E B]]

[[Category: Holmes, W]]

[[Category: Lovejoy, B]]

[[Category: Montana, V G]]

[[Category: Piwnica-Worms, H]]

[[Category: Rink, M J]]

[[Category: Rocque, W J]]

[[Category: Saper, M A]]

[[Category: Hydrolase]]