2rqy

From Proteopedia

(Difference between revisions)

Current revision

Solution structure and dynamics of mouse ARMET

Structural highlights

2rqy is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 10 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hoseki J, Sasakawa H, Yamaguchi Y, Maeda M, Kubota H, Kato K, Nagata K. Solution structure and dynamics of mouse ARMET. FEBS Lett. 2010 Apr 16;584(8):1536-42. Epub 2010 Mar 6. PMID:20214902 doi:10.1016/j.febslet.2010.03.008

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rqy"

@@ Line 1: / Line 1: @@
 ==Solution structure and dynamics of mouse ARMET==
-<StructureSection load='2rqy' size='340' side='right' caption='[[2rqy]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2rqy' size='340' side='right'caption='[[2rqy]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rqy]] is a 1 chain structure with sequence from [http://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=2RQY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RQY FirstGlance]. <br>
+<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>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Armet, mCG_19507 ([http://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, 10 models</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=2rqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rqy OCA], [http://pdbe.org/2rqy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rqy RCSB], [http://www.ebi.ac.uk/pdbsum/2rqy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rqy 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=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>
 </table>
+== Function ==
+[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]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 12: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rq/2rqy_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 30: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Hoseki, J]]
+[[Category: Mus musculus]]
-[[Category: Kato, K]]
+[[Category: Hoseki J]]
-[[Category: Kubota, H]]
+[[Category: Kato K]]
-[[Category: Maeda, M]]
+[[Category: Kubota H]]
-[[Category: Nagata, K]]
+[[Category: Maeda M]]
-[[Category: Sasakawa, H]]
+[[Category: Nagata K]]
-[[Category: Yamaguchi, Y]]
+[[Category: Sasakawa H]]
-[[Category: Cxxc motif]]
+[[Category: Yamaguchi Y]]
-[[Category: Endoplasmic reticulum]]
-[[Category: Unfolded protein response]]
-[[Category: Unknown function]]

2rqy

From Proteopedia

Current revision

Solution structure and dynamics of mouse ARMET

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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