2esb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:50, 13 March 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2esb.gif|left|200px]]
 
-
<!--
+
==Crystal structure of human DUSP18==
-
The line below this paragraph, containing "STRUCTURE_2esb", creates the "Structure Box" on the page.
+
<StructureSection load='2esb' size='340' side='right'caption='[[2esb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2esb]] 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=2ESB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ESB FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</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&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>
-
{{STRUCTURE_2esb| PDB=2esb | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2esb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2esb OCA], [https://pdbe.org/2esb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2esb RCSB], [https://www.ebi.ac.uk/pdbsum/2esb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2esb ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/DUS18_HUMAN DUS18_HUMAN] Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/2esb_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=2esb ConSurf].
 +
<div style="clear:both"></div>
-
'''Crystal structure of human DUSP18'''
+
==See Also==
-
 
+
*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
The human dual-specificity protein phosphatase 18 (DSP18) gene and its protein product have recently been characterized. Like most DSPs, DSP18 displays dephosphorylating activity towards both phosphotyrosine and phosphothreonine residues. However, DSP18 is distinct from other known DSPs in terms of the existence of approximately 30 residues at the C-terminus of the catalytic domain and an unusual optimum activity profile at 328 K. The crystal structure of human DSP18 has been determined at 2.0 A resolution. The catalytic domain of DSP18 adopts a fold similar to that known for other DSP structures. Although good alignments are found with other DSPs, substantial differences are also found in the regions surrounding the active site, suggesting that DSP18 constitutes a unique structure with a distinct substrate specificity. Furthermore, the residues at the C-terminus fold into two antiparallel beta-strands and participate in extensive interactions with the catalytic domain, explaining the thermostability of DSP18.
+
-
 
+
-
==About this Structure==
+
-
2ESB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESB OCA].
+
-
 
+
-
==Reference==
+
-
Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family., Jeong DG, Cho YH, Yoon TS, Kim JH, Son JH, Ryu SE, Kim SJ, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):582-8. Epub 2006, May 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16699184 16699184]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Cho, Y H.]]
+
[[Category: Cho YH]]
-
[[Category: Jeong, D G.]]
+
[[Category: Jeong DG]]
-
[[Category: Kim, J H.]]
+
[[Category: Kim JH]]
-
[[Category: Kim, S J.]]
+
[[Category: Kim SJ]]
-
[[Category: Ryu, S E.]]
+
[[Category: Ryu SE]]
-
[[Category: Yoon, T S.]]
+
[[Category: Yoon TS]]
-
[[Category: Alpha/beta structure]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:03:34 2008''
+

Current revision

Crystal structure of human DUSP18

PDB ID 2esb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2esb"
Personal tools