2mv6: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[2mv6]] 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=2MV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MV6 FirstGlance]. <br>
-</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=2mv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mv6 OCA], [https://pdbe.org/2mv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mv6 RCSB], [https://www.ebi.ac.uk/pdbsum/2mv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mv6 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mv6 OCA], [https://pdbe.org/2mv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mv6 RCSB], [https://www.ebi.ac.uk/pdbsum/2mv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mv6 ProSAT]</span></td></tr>
 </table>
 == Disease ==
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 == Function ==
 [https://www.uniprot.org/uniprot/EPOR_HUMAN EPOR_HUMAN] Receptor for erythropoietin. Mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase.  Isoform EPOR-T acts as a dominant-negative receptor of EPOR-mediated signaling.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Erythropoietin receptor (EpoR) dimerization is an important step in erythrocyte formation. Its transmembrane domain (TMD) and juxtamembrane (JM) region are essential for signal transduction across the membrane. A construct compassing residues S212-P259 and containing the TMD and JM region of the human EpoR was purified and reconstituted in detergent micelles. The solution structure of the construct was determined in dodecylphosphocholine (DPC) micelles by solution NMR spectroscopy. Structural and dynamic studies demonstrated that the TMD and JM region are an ?-helix in DPC micelles, whereas residues S212-D224 at the N-terminus of the construct are not structured. The JM region is a helix that contains a hydrophobic patch formed by conserved hydrophobic residues (L253, I257, and W258). Nuclear Overhauser effect analysis, fluorescence spectroscopy, and paramagnetic relaxation enhancement experiments suggested that the JM region is exposed to the solvent. The structures of the TMD and JM region of the mouse EpoR were similar to those of the human EpoR.
-Structural insight into the transmembrane domain and the juxtamembrane region of the erythropoietin receptor in micelles.,Li Q, Wong YL, Huang Q, Kang C Biophys J. 2014 Nov 18;107(10):2325-36. doi: 10.1016/j.bpj.2014.10.013. PMID:25418301<ref>PMID:25418301</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2mv6" style="background-color:#fffaf0;"></div>
 ==See Also==