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| | ==DnaJB1 JD-GF== | | ==DnaJB1 JD-GF== |
| - | <StructureSection load='6z5n' size='340' side='right'caption='[[6z5n]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='6z5n' size='340' side='right'caption='[[6z5n]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6z5n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z5N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Z5N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6z5n]] 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=6Z5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z5N FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNAJB1, DNAJ1, HDJ1, HSPF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=6z5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z5n OCA], [https://pdbe.org/6z5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z5n RCSB], [https://www.ebi.ac.uk/pdbsum/6z5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z5n ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6z5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z5n OCA], [http://pdbe.org/6z5n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6z5n RCSB], [http://www.ebi.ac.uk/pdbsum/6z5n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6z5n ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DNJB1_HUMAN DNJB1_HUMAN]] Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. | + | [https://www.uniprot.org/uniprot/DNJB1_HUMAN DNJB1_HUMAN] Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6z5n" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6z5n" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]] |
| | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Avraham-Abayev, M]] | + | [[Category: Avraham-Abayev M]] |
| - | [[Category: London, N]] | + | [[Category: London N]] |
| - | [[Category: Rosenzweig, R]] | + | [[Category: Rosenzweig R]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Dnaj]]
| + | |
| - | [[Category: Hsp40]]
| + | |
| - | [[Category: J-domain protein]]
| + | |
| - | [[Category: Molecular chaperone]]
| + | |
| Structural highlights
Function
DNJB1_HUMAN Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.
Publication Abstract from PubMed
The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular chaperones, which perform numerous cellular functions that affect almost all aspects of the protein life cycle from synthesis to degradation(1-3). Achieving this broad spectrum of functions requires precise regulation of HSP70 activity. Proteins of the HSP40 family, also known as J-domain proteins (JDPs), have a key role in this process by preselecting substrates for transfer to their HSP70 partners and by stimulating the ATP hydrolysis of HSP70, leading to stable substrate binding(3,4). In humans, JDPs constitute a large and diverse family with more than 40 different members(2), which vary in their substrate selectivity and in the nature and number of their client-binding domains(5). Here we show that JDPs can also differ fundamentally in their interactions with HSP70 chaperones. Using nuclear magnetic resonance spectroscopy(6,7) we find that the major class B JDPs are regulated by an autoinhibitory mechanism that is not present in other classes. Although in all JDPs the interaction of the characteristic J-domain is responsible for the activation of HSP70, in DNAJB1 the HSP70-binding sites in this domain are intrinsically blocked by an adjacent glycine-phenylalanine rich region-an inhibition that can be released upon the interaction of a second site on DNAJB1 with the HSP70 C-terminal tail. This regulation, which controls substrate targeting to HSP70, is essential for the disaggregation of amyloid fibres by HSP70-DNAJB1, illustrating why no other class of JDPs can substitute for class B in this function. Moreover, this regulatory layer, which governs the functional specificities of JDP co-chaperones and their interactions with HSP70s, could be key to the wide range of cellular functions of HSP70.
HSP40 proteins use class-specific regulation to drive HSP70 functional diversity.,Faust O, Abayev-Avraham M, Wentink AS, Maurer M, Nillegoda NB, London N, Bukau B, Rosenzweig R Nature. 2020 Nov;587(7834):489-494. doi: 10.1038/s41586-020-2906-4. Epub 2020 Nov, 11. PMID:33177718[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Faust O, Abayev-Avraham M, Wentink AS, Maurer M, Nillegoda NB, London N, Bukau B, Rosenzweig R. HSP40 proteins use class-specific regulation to drive HSP70 functional diversity. Nature. 2020 Nov;587(7834):489-494. doi: 10.1038/s41586-020-2906-4. Epub 2020 Nov, 11. PMID:33177718 doi:http://dx.doi.org/10.1038/s41586-020-2906-4
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