We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2img

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:13, 30 October 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2img.gif|left|200px]]
 
-
<!--
+
==Crystal structure of dual specificity protein phosphatase 23 from Homo sapiens in complex with ligand malate ion==
-
The line below this paragraph, containing "STRUCTURE_2img", creates the "Structure Box" on the page.
+
<StructureSection load='2img' size='340' side='right'caption='[[2img]], [[Resolution|resolution]] 1.93&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'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IMG 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]] 1.93&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
{{STRUCTURE_2img| PDB=2img | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2img FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2img OCA], [https://pdbe.org/2img PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2img RCSB], [https://www.ebi.ac.uk/pdbsum/2img PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2img ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2img TOPSAN]</span></td></tr>
 +
</table>
 +
== 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/im/2img_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2img ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Protein phosphorylation plays a crucial role in mitogenic signal transduction and regulation of cell growth and differentiation. Dual specificity protein phosphatase 23 (DUSP23) or VHZ mediates dephosphorylation of phospho-tyrosyl (pTyr) and phospho-seryl/threonyl (pSer/pThr) residues in specific proteins. In vitro, it can dephosphorylate p44ERK1 but not p54SAPK-beta and enhance activation of c-Jun N-terminal kinase (JNK) and p38. Human VHZ, the smallest of the catalytically active protein-tyrosine phosphatases (PTP) reported to date (150 residues), is a class I Cys-based PTP and bears the distinctive active site signature motif HCXXGXXRS(T). We present the crystal structure of VHZ determined at 1.93A resolution. The polypeptide chain adopts the typical alphabetaalpha PTP fold, giving rise to a shallow active site cleft that supports dual phosphorylated substrate specificity. Within our crystals, the Thr-135-Tyr-136 from a symmetry-related molecule bind in the active site with a malate ion, where they mimic the phosphorylated TY motif of the MAPK activation loop in an enzyme-substrate/product complex. Analyses of intermolecular interactions between the enzyme and this pseudo substrate/product along with functional analysis of Phe-66, Leu-97, and Phe-99 residues provide insights into the mechanism of substrate binding and catalysis in VHZ.
-
'''Crystal structure of dual specificity protein phosphatase 23 from Homo sapiens in complex with ligand malate ion'''
+
Structure of human dual specificity protein phosphatase 23, VHZ, enzyme-substrate/product complex.,Agarwal R, Burley SK, Swaminathan S J Biol Chem. 2008 Apr 4;283(14):8946-53. Epub 2008 Feb 1. PMID:18245086<ref>PMID:18245086</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2img" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases.
+
*[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]]
-
 
+
*[[MAP kinase phosphatase|MAP kinase phosphatase]]
-
==About this Structure==
+
== References ==
-
2IMG 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=2IMG OCA].
+
<references/>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structural genomics of protein phosphatases., Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK, J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18058037 18058037]
+
[[Category: Large Structures]]
-
[[Category: Homo sapiens]]
+
[[Category: Agarwal R]]
-
[[Category: Single protein]]
+
[[Category: Burley SK]]
-
[[Category: Agarwal, R.]]
+
[[Category: Swaminathan S]]
-
[[Category: Burley, S K.]]
+
-
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
+
-
[[Category: Swaminathan, S.]]
+
-
[[Category: 8673a]]
+
-
[[Category: Dual specicity protein phosphatase 23]]
+
-
[[Category: Dus23_human]]
+
-
[[Category: Dusp23]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Ldp-3]]
+
-
[[Category: Malate]]
+
-
[[Category: New york structural genomix research consortium]]
+
-
[[Category: Nysgxrc]]
+
-
[[Category: Protein structure initiative]]
+
-
[[Category: Psi]]
+
-
[[Category: Structural genomic]]
+
-
[[Category: Vhz]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:39:20 2008''
+

Current revision

Crystal structure of dual specificity protein phosphatase 23 from Homo sapiens in complex with ligand malate ion

PDB ID 2img

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/2img"
Personal tools