2wgp: Difference between revisions

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<StructureSection load='2wgp' size='340' side='right'caption='[[2wgp]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
<StructureSection load='2wgp' size='340' side='right'caption='[[2wgp]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2wgp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WGP FirstGlance]. <br>
<table><tr><td colspan='2'>[[2wgp]] 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=2WGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WGP FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wgp OCA], [https://pdbe.org/2wgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wgp RCSB], [https://www.ebi.ac.uk/pdbsum/2wgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wgp 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=2wgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wgp OCA], [https://pdbe.org/2wgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wgp RCSB], [https://www.ebi.ac.uk/pdbsum/2wgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wgp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DUS14_HUMAN DUS14_HUMAN]] Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.  
[https://www.uniprot.org/uniprot/DUS14_HUMAN DUS14_HUMAN] Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
*[[MAP kinase phosphatase|MAP kinase phosphatase]]
*[[MAP kinase phosphatase|MAP kinase phosphatase]]
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cherry, S]]
[[Category: Cherry S]]
[[Category: Lountos, G T]]
[[Category: Lountos GT]]
[[Category: Tropea, J E]]
[[Category: Tropea JE]]
[[Category: Waugh, D S]]
[[Category: Waugh DS]]
[[Category: Dual specificity phosphatase]]
[[Category: Dusp14]]
[[Category: Hydrolase]]
[[Category: Mkp6]]
[[Category: Protein phosphatase]]

Latest revision as of 18:55, 13 December 2023

Crystal structure of human dual specificity phosphatase 14Crystal structure of human dual specificity phosphatase 14

Structural highlights

2wgp is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.88Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DUS14_HUMAN Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Dual-specificity phosphatases (DUSPs) are enzymes that participate in the regulation of biological processes such as cell growth, differentiation, transcription and metabolism. A number of DUSPs are able to dephosphorylate phosphorylated serine, threonine and tyrosine residues on mitogen-activated protein kinases (MAPKs) and thus are also classified as MAPK phosphatases (MKPs). As an increasing number of DUSPs are being identified and characterized, there is a growing need to understand their biological activities at the molecular level. There is also significant interest in identifying DUSPs that could be potential targets for drugs that modulate MAPK-dependent signaling and immune responses, which have been implicated in a variety of maladies including cancer, infectious diseases and inflammatory disorders. Here, the overproduction, purification and crystal structure at 1.88 A resolution of human dual-specificity phosphatase 14, DUSP14 (MKP6), are reported. This structural information should accelerate the study of DUSP14 at the molecular level and may also accelerate the discovery and development of novel therapeutic agents.

Overproduction, purification and structure determination of human dual-specificity phosphatase 14.,Lountos GT, Tropea JE, Cherry S, Waugh DS Acta Crystallogr D Biol Crystallogr. 2009 Oct;65(Pt 10):1013-20. Epub 2009, Sep 16. PMID:19770498[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Lountos GT, Tropea JE, Cherry S, Waugh DS. Overproduction, purification and structure determination of human dual-specificity phosphatase 14. Acta Crystallogr D Biol Crystallogr. 2009 Oct;65(Pt 10):1013-20. Epub 2009, Sep 16. PMID:19770498 doi:10.1107/S0907444909023762

2wgp, resolution 1.88Å

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