1k36

<StructureSection load='1k36' size='340' side='right' caption='[[1k36]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1k36]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k37|1k37]]</td></tr>

<tr id='resources'><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://pdbe.org/1k36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k36 RCSB], [http://www.ebi.ac.uk/pdbsum/1k36 PDBsum]</span></td></tr>

[[http://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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/1k36_consurf.spt"</scriptWhenChecked>

</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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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1k36" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Aizawa, T]]

[[Category: Kawano, K]]

[[Category: Miura, K]]

[[Category: Miyamoto, K]]

[[Category: Sato, K]]

[[Category: Tada, M]]

[[Category: Hormone-growth factor complex]]