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==Structure of the transmembrane domain of the mouse erythropoietin receptor==
==Structure of the transmembrane domain of the mouse erythropoietin receptor==
<StructureSection load='2mxb' size='340' side='right'caption='[[2mxb]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2mxb' size='340' side='right'caption='[[2mxb]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mxb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MXB FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mxb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MXB FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Epor ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=2mxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mxb OCA], [https://pdbe.org/2mxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mxb RCSB], [https://www.ebi.ac.uk/pdbsum/2mxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mxb ProSAT]</span></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=2mxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mxb OCA], [https://pdbe.org/2mxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mxb RCSB], [https://www.ebi.ac.uk/pdbsum/2mxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mxb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/EPOR_MOUSE EPOR_MOUSE]] 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.<ref>PMID:8382775</ref> <ref>PMID:8617735</ref>
[https://www.uniprot.org/uniprot/EPOR_MOUSE EPOR_MOUSE] 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.<ref>PMID:8382775</ref> <ref>PMID:8617735</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Erythropoiesis is regulated by the erythropoietin receptor (EpoR) binding to its ligand. The transmembrane domain (TMD) and the juxtamembrane (JM) regions of the EpoR are important for signal transduction across the cell membrane. We report a solution NMR study of the mouse erythropoietin receptor (mEpoR) comprising the TMD and the JM regions reconstituted in dodecylphosphocholine (DPC) micelles. The TMD and the C-terminal JM region of the mEpoR are mainly alpha-helical, adopting a similar structure to those of the human EpoR. Residues from S216 to T219 in mEpoR form a short helix. Relaxation study demonstrates that the TMD of the mEpoR is rigid whilst the N-terminal region preceding the TMD is flexible. Fluorescence spectroscopy and sequence analysis indicate that the C-terminal JM region is exposed to the solvent. Helix wheel result shows that there is hydrophilic patch in the TMD of the mEpoR formed by residues S231, S238 and T242, and these residues might be important for the receptor dimerization.


Solution structure of the transmembrane domain of the mouse erythropoietin receptor in detergent micelles.,Li Q, Wong YL, Yueqi Lee M, Li Y, Kang C Sci Rep. 2015 Aug 28;5:13586. doi: 10.1038/srep13586. PMID:26316120<ref>PMID:26316120</ref>
==See Also==
 
*[[Erythropoietin receptor|Erythropoietin receptor]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mxb" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Kang, C]]
[[Category: Kang C]]
[[Category: Lee, M]]
[[Category: Lee M]]
[[Category: Li, Q]]
[[Category: Li Q]]
[[Category: Wong, Y]]
[[Category: Wong Y]]
[[Category: Membrane protein]]

Latest revision as of 07:02, 1 May 2024

Structure of the transmembrane domain of the mouse erythropoietin receptor

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