View source for 8dts


==X-ray crystal structure of AFSSFN from chaperone DNAJB8.==
<StructureSection load='8dts' size='340' side='right'caption='[[8dts]], [[Resolution|resolution]] 0.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8dts]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DTS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.75&#8491;</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=8dts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dts OCA], [https://pdbe.org/8dts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dts RCSB], [https://www.ebi.ac.uk/pdbsum/8dts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dts ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DNJB8_HUMAN DNJB8_HUMAN] Efficient suppressor of aggregation and toxicity of disease-associated polyglutamine proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
J-domain protein (JDP) molecular chaperones have emerged as central players that maintain a healthy proteome. The diverse members of the JDP family function as monomers/dimers and a small subset assemble into micron-sized oligomers. The oligomeric JDP members have eluded structural characterization due to their low-complexity, intrinsically disordered middle domains. This in turn, obscures the biological significance of these larger oligomers in protein folding processes. Here, we identified a short, aromatic motif within DNAJB8 that drives self-assembly through pi-pi stacking and determined its X-ray structure. We show that mutations in the motif disrupt DNAJB8 oligomerization in vitro and in cells. DNAJB8 variants that are unable to assemble bind to misfolded tau seeds more specifically and retain capacity to reduce protein aggregation in vitro and in cells. We propose a new model for DNAJB8 function in which the sequences in the low-complexity domains play distinct roles in assembly and substrate activity.

DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity.,Ryder BD, Ustyantseva E, Boyer DR, Mendoza-Oliva A, Kuska MI, Wydorski PM, Macierzynska P, Morgan N, Sawaya MR, Diamond MI, Kampinga HH, Joachimiak LA Structure. 2024 Jun 6;32(6):662-678.e8. doi: 10.1016/j.str.2024.02.015. Epub 2024 , Mar 19. PMID:38508190<ref>PMID:38508190</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8dts" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Boyer DR]]
[[Category: Joachimiak LA]]
[[Category: Ryder B]]
[[Category: Sawaya MR]]