2gwo: Difference between revisions

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<StructureSection load='2gwo' size='340' side='right'caption='[[2gwo]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2gwo' size='340' side='right'caption='[[2gwo]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2gwo]] is a 4 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=2GWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GWO FirstGlance]. <br>
<table><tr><td colspan='2'>[[2gwo]] is a 4 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=2GWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GWO FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DUSP13, TMDP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.4&#8491;</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=2gwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gwo OCA], [https://pdbe.org/2gwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gwo RCSB], [https://www.ebi.ac.uk/pdbsum/2gwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gwo 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=2gwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gwo OCA], [https://pdbe.org/2gwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gwo RCSB], [https://www.ebi.ac.uk/pdbsum/2gwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gwo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DS13B_HUMAN DS13B_HUMAN]] Dual specificity phosphatase that dephosphorylates MAPK8/JNK and MAPK14/p38, but not MAPK1/ERK2, in vitro. Exhibits intrinsic phosphatase activity towards both phospho-seryl/threonyl and -tyrosyl residues, with similar specific activities in vitro.<ref>PMID:21360282</ref>
[https://www.uniprot.org/uniprot/DS13B_HUMAN DS13B_HUMAN] Dual specificity phosphatase that dephosphorylates MAPK8/JNK and MAPK14/p38, but not MAPK1/ERK2, in vitro. Exhibits intrinsic phosphatase activity towards both phospho-seryl/threonyl and -tyrosyl residues, with similar specific activities in vitro.<ref>PMID:21360282</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gwo ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gwo ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The testis- and skeletal-muscle-specific dual-specificity phosphatase (TMDP) is a member of the dual-specificity phosphatase (DSP) subgroup of protein tyrosine phosphatases. TMDP has similar activities toward both tyrosine and threonine phosphorylated substrates, and is supposed to be involved in spermatogenesis. Here, we report the crystal structure of human TMDP at a resolution of 2.4 A. In spite of high sequence similarity with other DSPs, the crystal structure of TMDP shows distinct structural motifs and surface properties. In TMDP, the alpha1-beta1 loop, a substrate recognition motif is located further away from the active site loop in comparison to prototype DSP Vaccinia H1 related phophatase (VHR), which preferentially dephosphorylates tyrosine phosphorylated substrates and down-regulates MAP kinase signaling. Residues in the active site residues of TMDP are smaller in size and more hydrophobic than those of VHR. In addition, TMDP cannot be aligned with VHR in loop beta3-alpha4. These differences in the active site of TMDP result in a flat and wide pocket structure, allowing equal binding of phosphotyrosine and phosphothreonine substrates.
Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity.,Kim SJ, Jeong DG, Yoon TS, Son JH, Cho SK, Ryu SE, Kim JH Proteins. 2007 Jan 1;66(1):239-45. PMID:17044055<ref>PMID:17044055</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2gwo" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[MAP kinase phosphatase|MAP kinase 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: Large Structures]]
[[Category: Large Structures]]
[[Category: Kim, J H]]
[[Category: Kim JH]]
[[Category: Kim, S J]]
[[Category: Kim SJ]]
[[Category: Ryu, S E]]
[[Category: Ryu SE]]
[[Category: Alpha/beta]]
[[Category: Hydrolase]]

Latest revision as of 16:52, 13 March 2024

crystal structure of TMDPcrystal structure of TMDP

Structural highlights

2gwo is a 4 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 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DS13B_HUMAN Dual specificity phosphatase that dephosphorylates MAPK8/JNK and MAPK14/p38, but not MAPK1/ERK2, in vitro. Exhibits intrinsic phosphatase activity towards both phospho-seryl/threonyl and -tyrosyl residues, with similar specific activities in vitro.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Katagiri C, Masuda K, Nomura M, Tanoue K, Fujita S, Yamashita Y, Katakura R, Shiiba K, Nomura E, Sato M, Tanuma N, Shima H. DUSP13B/TMDP inhibits stress-activated MAPKs and suppresses AP-1-dependent gene expression. Mol Cell Biochem. 2011 Jun;352(1-2):155-62. doi: 10.1007/s11010-011-0749-x. Epub , 2011 Mar 1. PMID:21360282 doi:http://dx.doi.org/10.1007/s11010-011-0749-x

2gwo, resolution 2.40Å

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