1k36

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[[Image:1k36.png|left|200px]]
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==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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== 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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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k37|1k37]]</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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<table>
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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/k3/1k36_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/chain_selection.php?pdb_ID=2ata ConSurf].
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<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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{{STRUCTURE_1k36| PDB=1k36 | SCENE= }}
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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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===NMR Structure of human Epiregulin===
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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>
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{{ABSTRACT_PUBMED_14572630}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:014572630</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Aizawa, T.]]
[[Category: Aizawa, T.]]

Revision as of 12:30, 28 September 2014

NMR Structure of human Epiregulin

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