2m66

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==Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: 3D Protein Fold Determination from Backbone Amide Pseudocontact Shifts Generated by Lanthanide Tags at Multiple Sites==
==Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: 3D Protein Fold Determination from Backbone Amide Pseudocontact Shifts Generated by Lanthanide Tags at Multiple Sites==
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<StructureSection load='2m66' size='340' side='right'caption='[[2m66]], [[NMR_Ensembles_of_Models | 11 NMR models]]' scene=''>
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<StructureSection load='2m66' size='340' side='right'caption='[[2m66]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2m66]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M66 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2m66]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M66 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g7d|1g7d]]</div></td></tr>
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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</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Erp29 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=2m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m66 OCA], [https://pdbe.org/2m66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m66 RCSB], [https://www.ebi.ac.uk/pdbsum/2m66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m66 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=2m66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m66 OCA], [https://pdbe.org/2m66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m66 RCSB], [https://www.ebi.ac.uk/pdbsum/2m66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m66 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ERP29_RAT ERP29_RAT]] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.
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[https://www.uniprot.org/uniprot/ERP29_RAT ERP29_RAT] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Site-specific attachment of paramagnetic lanthanide ions to a protein generates pseudocontact shifts (PCS) in the nuclear magnetic resonance (NMR) spectra of the protein that are easily measured as changes in chemical shifts. By labeling the protein with lanthanide tags at four different sites, PCSs are observed for most amide protons and accurate information is obtained about their coordinates in three-dimensional space. The approach is demonstrated with the chaperone ERp29, for which large differences have been reported between X-ray and NMR structures of the C-terminal domain, ERp29-C. The results unambiguously show that the structure of rat ERp29-C in solution is similar to the crystal structure of human ERp29-C. PCSs of backbone amides were the only structural restraints required. Because these can be measured for more dilute protein solutions than other NMR restraints, the approach greatly widens the range of proteins amenable to structural studies in solution.
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Three-dimensional protein fold determination from backbone amide pseudocontact shifts generated by lanthanide tags at multiple sites.,Yagi H, Pilla KB, Maleckis A, Graham B, Huber T, Otting G Structure. 2013 Jun 4;21(6):883-90. doi: 10.1016/j.str.2013.04.001. Epub 2013 May, 2. PMID:23643949<ref>PMID:23643949</ref>
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==See Also==
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*[[ER-resident protein|ER-resident protein]]
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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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<div class="pdbe-citations 2m66" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Graham, B]]
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[[Category: Rattus norvegicus]]
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[[Category: Huber, T]]
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[[Category: Graham B]]
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[[Category: Maleckis, A]]
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[[Category: Huber T]]
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[[Category: Otting, G]]
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[[Category: Maleckis A]]
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[[Category: Pilla, K]]
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[[Category: Otting G]]
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[[Category: Yagi, H]]
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[[Category: Pilla K]]
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[[Category: Chaperone]]
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[[Category: Yagi H]]
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[[Category: Erp29]]
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[[Category: Erp29-c]]
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[[Category: Gps-rosetta]]
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Current revision

Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: 3D Protein Fold Determination from Backbone Amide Pseudocontact Shifts Generated by Lanthanide Tags at Multiple Sites

PDB ID 2m66

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