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| | ==Crystal structure of the catalytic domain of human DUSP12 at 2.0 A resolution== | | ==Crystal structure of the catalytic domain of human DUSP12 at 2.0 A resolution== |
| - | <StructureSection load='4ki9' size='340' side='right' caption='[[4ki9]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4ki9' size='340' side='right'caption='[[4ki9]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ki9]] 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=4KI9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KI9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ki9]] 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=4KI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KI9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jnb|4jnb]]</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=4ki9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ki9 OCA], [https://pdbe.org/4ki9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ki9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ki9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ki9 ProSAT]</span></td></tr> |
| - | <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>
| + | |
| - | <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=4ki9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ki9 OCA], [http://pdbe.org/4ki9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ki9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ki9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ki9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DUS12_HUMAN DUS12_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Tyrosine phosphatase|Tyrosine phosphatase]] | + | *[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Chien, P N]] | + | [[Category: Large Structures]] |
| - | [[Category: Jeon, T J]] | + | [[Category: Chien PN]] |
| - | [[Category: Kim, S J]] | + | [[Category: Jeon TJ]] |
| - | [[Category: Ku, B]] | + | [[Category: Kim SJ]] |
| - | [[Category: Ryu, S E]] | + | [[Category: Ku B]] |
| - | [[Category: Dual specificity phosphatase]] | + | [[Category: Ryu SE]] |
| - | [[Category: Dusp]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protein tyrosine phosphatase]]
| + | |
| - | [[Category: Ptp]]
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| Structural highlights
Function
DUS12_HUMAN
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. The family-wide structure and function of human dual-specificity protein phosphatases. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):421-35. doi:, 10.1107/S1399004713029866. Epub 2014 Jan 29. PMID:24531476 doi:http://dx.doi.org/10.1107/S1399004713029866
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