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[[Image:1oem.jpg|left|200px]]
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{{STRUCTURE_1oem|  PDB=1oem  |  SCENE=  }}
'''PTP1B WITH THE CATALYTIC CYSTEINE OXIDIZED TO A SULFENYL-AMIDE BOND'''


==PTP1B with the catalytic cysteine oxidized to a sulfenyl-amide bond==
<StructureSection load='1oem' size='340' side='right'caption='[[1oem]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oem]] 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=1OEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OEM 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]] 1.8&#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=1oem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oem OCA], [https://pdbe.org/1oem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oem RCSB], [https://www.ebi.ac.uk/pdbsum/1oem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oem ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
== 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/oe/1oem_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=1oem ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The second messenger hydrogen peroxide is required for optimal activation of numerous signal transduction pathways, particularly those mediated by protein tyrosine kinases. One mechanism by which hydrogen peroxide regulates cellular processes is the transient inhibition of protein tyrosine phosphatases through the reversible oxidization of their catalytic cysteine, which suppresses protein dephosphorylation. Here we describe a structural analysis of the redox-dependent regulation of protein tyrosine phosphatase 1B (PTP1B), which is reversibly inhibited by oxidation after cells are stimulated with insulin and epidermal growth factor. The sulphenic acid intermediate produced in response to PTP1B oxidation is rapidly converted into a previously unknown sulphenyl-amide species, in which the sulphur atom of the catalytic cysteine is covalently linked to the main chain nitrogen of an adjacent residue. Oxidation of PTP1B to the sulphenyl-amide form is accompanied by large conformational changes in the catalytic site that inhibit substrate binding. We propose that this unusual protein modification both protects the active-site cysteine residue of PTP1B from irreversible oxidation to sulphonic acid and permits redox regulation of the enzyme by promoting its reversible reduction by thiols.


==Overview==
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate.,Salmeen A, Andersen JN, Myers MP, Meng TC, Hinks JA, Tonks NK, Barford D Nature. 2003 Jun 12;423(6941):769-73. PMID:12802338<ref>PMID:12802338</ref>
The second messenger hydrogen peroxide is required for optimal activation of numerous signal transduction pathways, particularly those mediated by protein tyrosine kinases. One mechanism by which hydrogen peroxide regulates cellular processes is the transient inhibition of protein tyrosine phosphatases through the reversible oxidization of their catalytic cysteine, which suppresses protein dephosphorylation. Here we describe a structural analysis of the redox-dependent regulation of protein tyrosine phosphatase 1B (PTP1B), which is reversibly inhibited by oxidation after cells are stimulated with insulin and epidermal growth factor. The sulphenic acid intermediate produced in response to PTP1B oxidation is rapidly converted into a previously unknown sulphenyl-amide species, in which the sulphur atom of the catalytic cysteine is covalently linked to the main chain nitrogen of an adjacent residue. Oxidation of PTP1B to the sulphenyl-amide form is accompanied by large conformational changes in the catalytic site that inhibit substrate binding. We propose that this unusual protein modification both protects the active-site cysteine residue of PTP1B from irreversible oxidation to sulphonic acid and permits redox regulation of the enzyme by promoting its reversible reduction by thiols.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1OEM 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=1OEM OCA].
</div>
<div class="pdbe-citations 1oem" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate., Salmeen A, Andersen JN, Myers MP, Meng TC, Hinks JA, Tonks NK, Barford D, Nature. 2003 Jun 12;423(6941):769-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12802338 12802338]
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Andersen JN]]
[[Category: Andersen, J N.]]
[[Category: Barford D]]
[[Category: Barford, D.]]
[[Category: Hinks JA]]
[[Category: Hinks, J A.]]
[[Category: Meng TC]]
[[Category: Meng, T C.]]
[[Category: Myers MP]]
[[Category: Myers, M P.]]
[[Category: Salmeen A]]
[[Category: Salmeen, A.]]
[[Category: Tonks NK]]
[[Category: Tonks, N K.]]
[[Category: Hydrolase,phosphorylation,phosphatase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:45:02 2008''
Retrieved from "https://proteopedia.org/1oem"