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1k36

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==NMR Structure of human Epiregulin==
==NMR Structure of human Epiregulin==
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<StructureSection load='1k36' size='340' side='right' caption='[[1k36]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
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<StructureSection load='1k36' size='340' side='right'caption='[[1k36]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1k36]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K36 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1k36]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K36 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k37|1k37]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k36 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k36 RCSB], [http://www.ebi.ac.uk/pdbsum/1k36 PDBsum]</span></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=1k36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k36 OCA], [https://pdbe.org/1k36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k36 RCSB], [https://www.ebi.ac.uk/pdbsum/1k36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k36 ProSAT]</span></td></tr>
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<table>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EREG_HUMAN EREG_HUMAN] Ligand of the EGF receptor/EGFR and ERBB4. May be a mediator of localized cell proliferation. As a mitogen it may stimulate cell proliferation and/or angiogenesis.<ref>PMID:9419975</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/1k36_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/1k36_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=1k36 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the receptors is lower than those of other EGF-family ligands. The solution structure of EPR was determined using two-dimensional nuclear magnetic resonance spectroscopy. The secondary structure in the C-terminal domain of EPR is different from other EGF-family ligands because of the lack of hydrogen bonds. The structural difference in the C-terminal domain may provide an explanation for the reduced binding affinity of EPR to the ErbB receptors.
 
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Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity.,Sato K, Nakamura T, Mizuguchi M, Miura K, Tada M, Aizawa T, Gomi T, Miyamoto K, Kawano K FEBS Lett. 2003 Oct 23;553(3):232-8. PMID:14572630<ref>PMID:14572630</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Aizawa, T.]]
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[[Category: Large Structures]]
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[[Category: Kawano, K.]]
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[[Category: Aizawa T]]
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[[Category: Miura, K.]]
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[[Category: Kawano K]]
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[[Category: Miyamoto, K.]]
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[[Category: Miura K]]
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[[Category: Sato, K.]]
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[[Category: Miyamoto K]]
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[[Category: Tada, M.]]
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[[Category: Sato K]]
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[[Category: Egf-like fold]]
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[[Category: Tada M]]
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[[Category: Hormone-growth factor complex]]
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Current revision

NMR Structure of human Epiregulin

PDB ID 1k36

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