7jsq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Refined structure of the C-terminal domain of DNAJB6b== |
| + | <StructureSection load='7jsq' size='340' side='right'caption='[[7jsq]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7jsq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JSQ FirstGlance]. <br> | ||
| + | </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=7jsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jsq OCA], [https://pdbe.org/7jsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jsq RCSB], [https://www.ebi.ac.uk/pdbsum/7jsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jsq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN] Autosomal dominant limb-girdle muscular dystrophy type 1D. The disease is caused by mutations affecting the gene represented in this entry. There is evidence that LGMDD1 is caused by dysfunction of isoform B (PubMed:22366786).<ref>PMID:22366786</ref> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DNJB6_HUMAN DNJB6_HUMAN] Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. Isoform B but not isoform A inhibits huntingtin aggregation. Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity.<ref>PMID:10954706</ref> <ref>PMID:11896048</ref> <ref>PMID:20159555</ref> <ref>PMID:22366786</ref> <ref>PMID:28233300</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]] | |
| - | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | |
| - | [[Category: | + | == References == |
| - | [[Category: Clore | + | <references/> |
| - | [[Category: Karamanos | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Clore GM]] | ||
| + | [[Category: Karamanos TK]] | ||
Current revision
Refined structure of the C-terminal domain of DNAJB6b
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