4jmk: Difference between revisions
New page: '''Unreleased structure''' The entry 4jmk is ON HOLD Authors: Dae Gwin, Jeong, Seung Jun, Kim, Seong Eon, Ryu Description: structure of dusp8 |
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The | ==Structure of dusp8== | ||
<StructureSection load='4jmk' size='340' side='right'caption='[[4jmk]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jmk]] is a 2 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=4JMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JMK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jmk OCA], [https://pdbe.org/4jmk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jmk RCSB], [https://www.ebi.ac.uk/pdbsum/4jmk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jmk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DUS8_HUMAN DUS8_HUMAN] This protein shows both activity toward tyrosine-protein phosphate as well as with serine/threonine-protein phosphate (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24531476</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4jmk" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[MAP kinase phosphatase|MAP kinase phosphatase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Jeong DG]] | |||
[[Category: Kim SJ]] | |||
[[Category: Ryu SE]] | |||
Latest revision as of 17:24, 8 November 2023
Structure of dusp8Structure of dusp8
Structural highlights
FunctionDUS8_HUMAN This protein shows both activity toward tyrosine-protein phosphate as well as with serine/threonine-protein phosphate (By similarity). Publication Abstract from PubMedDual-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 AlsoReferences
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