|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==NMR STRUCTURE OF N-DOMAIN OF ERP29 PROTEIN== | | ==NMR STRUCTURE OF N-DOMAIN OF ERP29 PROTEIN== |
| - | <StructureSection load='1g7e' size='340' side='right'caption='[[1g7e]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1g7e' size='340' side='right'caption='[[1g7e]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1g7e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G7E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1g7e]] 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=1G7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G7E FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g7d|1g7d]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g7e OCA], [http://pdbe.org/1g7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g7e RCSB], [http://www.ebi.ac.uk/pdbsum/1g7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g7e 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=1g7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g7e OCA], [https://pdbe.org/1g7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g7e RCSB], [https://www.ebi.ac.uk/pdbsum/1g7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g7e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 28: |
Line 28: |
| | </div> | | </div> |
| | <div class="pdbe-citations 1g7e" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1g7e" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ER-resident protein|ER-resident protein]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barishev, M]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Ingelman-Sundberg, M]] | + | [[Category: Barishev M]] |
| - | [[Category: Liepinsh, E]] | + | [[Category: Ingelman-Sundberg M]] |
| - | [[Category: Mkrtchian, S]] | + | [[Category: Liepinsh E]] |
| - | [[Category: Otting, G]] | + | [[Category: Mkrtchian S]] |
| - | [[Category: Sharipo, M]] | + | [[Category: Otting G]] |
| - | [[Category: Alfa-beta structure]]
| + | [[Category: Sharipo M]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Thioredoxin fold]]
| + | |
| Structural highlights
Function
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.
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
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, Mkrtchian S. Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer. Structure. 2001 Jun;9(6):457-71. PMID:11435111
|
