1g1h

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(New page: 200px<br /> <applet load="1g1h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g1h, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1g1h.gif|left|200px]]<br />
 
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<applet load="1g1h" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1g1h, resolution 2.40&Aring;" />
 
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'''CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A BIS-PHOSPHORYLATED PEPTIDE (ETD(PTR)(PTR)RKGGKGLL) FROM THE INSULIN RECEPTOR KINASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A BIS-PHOSPHORYLATED PEPTIDE (ETD(PTR)(PTR)RKGGKGLL) FROM THE INSULIN RECEPTOR KINASE==
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The protein tyrosine phosphatase PTP1B is responsible for negatively, regulating insulin signaling by dephosphorylating the phosphotyrosine, residues of the insulin receptor kinase (IRK) activation segment. Here, by, integrating crystallographic, kinetic, and PTP1B peptide binding studies, we define the molecular specificity of this reaction. Extensive, interactions are formed between PTP1B and the IRK sequence encompassing, the tandem pTyr residues at 1162 and 1163 such that pTyr-1162 is selected, at the catalytic site and pTyr-1163 is located within an adjacent pTyr, recognition site. This selectivity is attributed to the 70-fold greater, affinity for tandem pTyr-containing peptides relative to mono-pTyr, peptides and predicts a hierarchical dephosphorylation process. Many, elements of the PTP1B-IRK interaction are unique to PTP1B, indicating that, it may be feasible to generate specific, small molecule inhibitors of this, interaction to treat diabetes and obesity.
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<StructureSection load='1g1h' size='340' side='right'caption='[[1g1h]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1g1h]] 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=1G1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1H FirstGlance]. <br>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1h OCA], [https://pdbe.org/1g1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1h RCSB], [https://www.ebi.ac.uk/pdbsum/1g1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/1g1h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1g1h ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known diseases associated with this structure: Abdominal body fat distribution, modifier of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176885 176885]], Insulin resistance, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176885 176885]]
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1G1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G1H OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B., Salmeen A, Andersen JN, Myers MP, Tonks NK, Barford D, Mol Cell. 2000 Dec;6(6):1401-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11163213 11163213]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Andersen JN]]
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[[Category: Andersen, J.N.]]
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[[Category: Barford D]]
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[[Category: Barford, D.]]
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[[Category: Myers MP]]
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[[Category: Myers, M.P.]]
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[[Category: Salmeen A]]
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[[Category: Salmeen, A.]]
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[[Category: Tonks NK]]
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[[Category: Tonks, N.K.]]
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[[Category: hydrolase (phosphorylation)]]
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[[Category: peptide complex]]
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[[Category: tyrosine phosphatase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:59:25 2007''
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Current revision

CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A BIS-PHOSPHORYLATED PEPTIDE (ETD(PTR)(PTR)RKGGKGLL) FROM THE INSULIN RECEPTOR KINASE

PDB ID 1g1h

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