2rqy

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(New page: '''Unreleased structure''' The entry 2rqy is ON HOLD Authors: Hoseki, J., Sasakawa, H., Yamaguchi, Y., Maeda, M., Kubota, H., Kato, K., Nagata, K. Description: Solution structure and d...)
Current revision (09:30, 6 November 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2rqy is ON HOLD
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==Solution structure and dynamics of mouse ARMET==
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<StructureSection load='2rqy' size='340' side='right'caption='[[2rqy]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2rqy]] 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=2RQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RQY FirstGlance]. <br>
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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, 10 models</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=2rqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rqy OCA], [https://pdbe.org/2rqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rqy RCSB], [https://www.ebi.ac.uk/pdbsum/2rqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rqy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MANF_MOUSE MANF_MOUSE] Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. Retained in the ER/sarcoplasmic reticulum (SR) through association with the endoplasmic reticulum chaperone protein HSPA5 under normal conditions. Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia. Following secretion by the ER/SR, directly binds to 3-O-sulfogalactosylceramide, a lipid sulfatide in the outer cell membrane of target cells. Sulfatide binding promotes its cellular uptake by endocytosis, and is required for its role in alleviating ER stress and cell toxicity under hypoxic and ER stress conditions.[UniProtKB:P0C5H9][UniProtKB:P55145]
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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/rq/2rqy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2rqy 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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ARMET is an endoplasmic reticulum (ER) stress-inducible protein that is required for maintaining cell viability under ER stress conditions. However, the exact molecular mechanisms by which ARMET protects cells are unknown. Here, we have analyzed the solution structure of ARMET. ARMET has an entirely alpha-helical structure, which is composed of two distinct domains. Positive charges are dispersed on the surfaces of both domains and across a linker structure. Trypsin digestion and (15)N relaxation experiments indicate that the tumbling of the N-terminal and C-terminal domains is effectively independent. These results suggest that ARMET may hold a negatively charged molecule using the two positively charged domains.
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Authors: Hoseki, J., Sasakawa, H., Yamaguchi, Y., Maeda, M., Kubota, H., Kato, K., Nagata, K.
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Solution structure and dynamics of mouse ARMET.,Hoseki J, Sasakawa H, Yamaguchi Y, Maeda M, Kubota H, Kato K, Nagata K FEBS Lett. 2010 Apr 16;584(8):1536-42. Epub 2010 Mar 6. PMID:20214902<ref>PMID:20214902</ref>
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Description: Solution structure and dynamics of mouse ARMET
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 3 09:12:10 2010''
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<div class="pdbe-citations 2rqy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Hoseki J]]
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[[Category: Kato K]]
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[[Category: Kubota H]]
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[[Category: Maeda M]]
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[[Category: Nagata K]]
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[[Category: Sasakawa H]]
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[[Category: Yamaguchi Y]]

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Solution structure and dynamics of mouse ARMET

PDB ID 2rqy

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