4jnb

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==Crystal structure of the Catalytic Domain of Human DUSP12==
==Crystal structure of the Catalytic Domain of Human DUSP12==
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<StructureSection load='4jnb' size='340' side='right' caption='[[4jnb]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='4jnb' size='340' side='right'caption='[[4jnb]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4jnb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JNB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JNB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4jnb]] 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=4JNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JNB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DUSP12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=4jnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jnb OCA], [http://pdbe.org/4jnb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jnb RCSB], [http://www.ebi.ac.uk/pdbsum/4jnb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jnb ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jnb OCA], [https://pdbe.org/4jnb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jnb RCSB], [https://www.ebi.ac.uk/pdbsum/4jnb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jnb ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/DUS12_HUMAN DUS12_HUMAN]
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Dual-specificity protein phosphatases (DUSPs), which dephosphorylate both phosphoserine/threonine and phosphotyrosine, play vital roles in immune activation, brain function and cell-growth signalling. A family-wide structural library of human DUSPs was constructed based on experimental structure determination supplemented with homology modelling. The catalytic domain of each individual DUSP has characteristic features in the active site and in surface-charge distribution, indicating substrate-interaction specificity. The active-site loop-to-strand switch occurs in a subtype-specific manner, indicating that the switch process is necessary for characteristic substrate interactions in the corresponding DUSPs. A comprehensive analysis of the activity-inhibition profile and active-site geometry of DUSPs revealed a novel role of the active-pocket structure in the substrate specificity of DUSPs. A structure-based analysis of redox responses indicated that the additional cysteine residues are important for the protection of enzyme activity. The family-wide structures of DUSPs form a basis for the understanding of phosphorylation-mediated signal transduction and the development of therapeutics.
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The family-wide structure and function of human dual-specificity protein phosphatases.,Jeong DG, Wei CH, Ku B, Jeon TJ, Chien PN, Kim JK, Park SY, Hwang HS, Ryu SY, Park H, Kim DS, Kim SJ, Ryu SE Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):421-35. doi:, 10.1107/S1399004713029866. Epub 2014 Jan 29. PMID:24531476<ref>PMID:24531476</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4jnb" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Tyrosine phosphatase|Tyrosine phosphatase]]
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*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Chien, P N]]
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[[Category: Large Structures]]
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[[Category: Jeon, T J]]
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[[Category: Chien PN]]
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[[Category: Kim, S J]]
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[[Category: Jeon TJ]]
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[[Category: Ku, B]]
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[[Category: Kim SJ]]
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[[Category: Ryu, S E]]
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[[Category: Ku B]]
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[[Category: Dual specificity phosphatase]]
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[[Category: Ryu SE]]
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[[Category: Dusp]]
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[[Category: Hydrolase]]
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[[Category: Phosphatase]]
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Current revision

Crystal structure of the Catalytic Domain of Human DUSP12

PDB ID 4jnb

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