1g7d

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{{Seed}}
 
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[[Image:1g7d.png|left|200px]]
 
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==NMR STRUCTURE OF ERP29 C-DOMAIN==
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The line below this paragraph, containing "STRUCTURE_1g7d", creates the "Structure Box" on the page.
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<StructureSection load='1g7d' size='340' side='right'caption='[[1g7d]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1g7d]] 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=1G7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G7D FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g7d OCA], [https://pdbe.org/1g7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g7d RCSB], [https://www.ebi.ac.uk/pdbsum/1g7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g7d ProSAT]</span></td></tr>
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{{STRUCTURE_1g7d| PDB=1g7d | SCENE= }}
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</table>
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== 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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== 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/g7/1g7d_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1g7d 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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BACKGROUND: ERp29 is a ubiquitously expressed rat endoplasmic reticulum (ER) protein conserved in mammalian species. Fold predictions suggest the presence of a thioredoxin-like domain homologous to the a domain of human protein disulfide isomerase (PDI) and a helical domain similar to the C-terminal domain of P5-like PDIs. As ERp29 lacks the double-cysteine motif essential for PDI redox activity, it is suggested to play a role in protein maturation and/or secretion related to the chaperone function of PDI. ERp29 self-associates into 51 kDa dimers and also higher oligomers. RESULTS: 3D structures of the N- and C-terminal domains determined by NMR spectroscopy confirmed the thioredoxin fold for the N-terminal domain and yielded a novel all-helical fold for the C-terminal domain. Studies of the full-length protein revealed a short, flexible linker between the two domains, homodimerization by the N-terminal domain, and the presence of interaction sites for the formation of higher molecular weight oligomers. A gadolinium-based relaxation agent is shown to present a sensitive tool for the identification of macromolecular interfaces by NMR. CONCLUSIONS: ERp29 is the first eukaryotic PDI-related protein for which the structures of all domains have been determined. Furthermore, an experimental model of the full-length protein and its association states was established. It is the first example of a protein where the thioredoxin fold was found to act as a specific homodimerization module, without covalent linkages or supporting interactions by further domains. A homodimerization module similar as in ERp29 may also be present in homodimeric human PDI.
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===NMR STRUCTURE OF ERP29 C-DOMAIN===
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Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.,Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, Mkrtchian S Structure. 2001 Jun;9(6):457-71. PMID:11435111<ref>PMID:11435111</ref>
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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 1g7d" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11435111}}, adds the Publication Abstract to the page
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*[[ER-resident protein|ER-resident protein]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11435111 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11435111}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1G7D is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7D OCA].
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==Reference==
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<ref group="xtra">PMID:11435111</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Barishev, M.]]
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[[Category: Barishev M]]
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[[Category: Ingelman-Sundberg, M.]]
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[[Category: Ingelman-Sundberg M]]
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[[Category: Liepinsh, E.]]
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[[Category: Liepinsh E]]
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[[Category: Mkrtchian, S.]]
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[[Category: Mkrtchian S]]
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[[Category: Otting, G.]]
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[[Category: Otting G]]
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[[Category: Sharipo, A.]]
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[[Category: Sharipo A]]
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[[Category: Alpha helical protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:41:49 2009''
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Current revision

NMR STRUCTURE OF ERP29 C-DOMAIN

PDB ID 1g7d

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