7qby
From Proteopedia
(Difference between revisions)
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<StructureSection load='7qby' size='340' side='right'caption='[[7qby]]' scene=''> | <StructureSection load='7qby' size='340' side='right'caption='[[7qby]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QBY FirstGlance]. <br> |
| - | </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=7qby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qby OCA], [https://pdbe.org/7qby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qby RCSB], [https://www.ebi.ac.uk/pdbsum/7qby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qby ProSAT]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=7qby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qby OCA], [https://pdbe.org/7qby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qby RCSB], [https://www.ebi.ac.uk/pdbsum/7qby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qby ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | DNAJB6 is a prime example of an anti-aggregation chaperone that functions as an oligomer. DNAJB6 oligomers are dynamic and subunit exchange is critical for inhibiting client protein aggregation. The T193A mutation in the C-terminal domain (CTD) of DNAJB6 reduces both chaperone self-oligomerization and anti-aggregation of client proteins, and has recently been linked to Parkinson's disease. Here, we show by NMR, including relaxation-based methods, that the T193A mutation has minimal effects on the structure of the beta-stranded CTD but increases the population and rate of formation of a partially folded state. The results can be rationalized in terms of beta-strand peptide plane flips that occur on a timescale of approximately 100 mus and lead to global changes in the overall pleat/flatness of the CTD, thereby altering its ability to oligomerize. These findings help forge a link between chaperone dynamics, oligomerization and anti-aggregation activity which may possibly lead to new therapeutic avenues tuned to target specific substrates. | ||
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| + | Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone.,Cawood EE, Clore GM, Karamanos TK Angew Chem Int Ed Engl. 2022 Mar 5:e202116403. doi: 10.1002/anie.202116403. PMID:35247211<ref>PMID:35247211</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7qby" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Refined structure of the T193A mutant in the C-terminal domain of DNAJB6b
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