DnaJ homolog
From Proteopedia
(Difference between revisions)
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | <ref>PMID:21638687</ref> to the rescue. | ||
== Function == | == Function == | ||
| - | '''DnaJ homolog subfamily A member 1''' (DnaJA1) is a co-chaperone for HSPA8/Hsc70. | + | '''DnaJ homolog subfamily A member 1''' (DnaJA1) is a co-chaperone for HSPA8/Hsc70. DnaJA1 stimulates ATP synthesis and has a role in protein transport into mitochondria<ref>PMID:10816573</ref>.<br /> |
| + | '''DnaJ homolog subfamily B member 1''' (DnaJB1) interacts with HSP70. DnaJB1 stimulates ATP synthesis and the folding of unfolded proteins mediated by HSPA1A <ref>PMID:24318877</ref>.<br /> | ||
== Disease == | == Disease == | ||
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*DnaJ homolog subfamily A member 1 | *DnaJ homolog subfamily A member 1 | ||
| - | **[[2l01]], [[2m6y]] - | + | **[[2l01]], [[2m6y]] - hDnaJA1 J domain - human - NMR<br /> |
*DnaJ homolog subfamily A member 3 | *DnaJ homolog subfamily A member 3 | ||
| - | **[[2dn9]] - | + | **[[2dn9]] - hDnaJA3 J domain - NMR<br /> |
**[[2ctt]] - hDnaJ zinc finger domain - NMR<br /> | **[[2ctt]] - hDnaJ zinc finger domain - NMR<br /> | ||
*DnaJ homolog subfamily B member 1 | *DnaJ homolog subfamily B member 1 | ||
| - | **[[3agx]], [[2qld]] - | + | **[[3agx]], [[2qld]] - hDnaJB1 peptide-binding domain <br /> |
| - | **[[3agy]], [[3agz]] - | + | **[[3agy]], [[3agz]] - hDnaJB1 peptide-binding domain + HSP70 peptide<br /> |
*DnaJ homolog subfamily B member 2 | *DnaJ homolog subfamily B member 2 | ||
| - | **[[2lgw]] - | + | **[[2lgw]] - hDnaJB2 J domain - NMR<br /> |
*DnaJ homolog subfamily B member 8 | *DnaJ homolog subfamily B member 8 | ||
| - | **[[2dmx]] - | + | **[[2dmx]] - hDnaJB8 J domain - NMR<br /> |
*DnaJ homolog subfamily B member 9 | *DnaJ homolog subfamily B member 9 | ||
| - | **[[2ctr]] - | + | **[[2ctr]] - hDnaJB9 J domain - NMR<br /> |
*DnaJ homolog subfamily B member 12 | *DnaJ homolog subfamily B member 12 | ||
| - | **[[2ctp]] - | + | **[[2ctp]] - hDnaJB12 J domain - NMR<br /> |
*DnaJ homolog subfamily C member 1 | *DnaJ homolog subfamily C member 1 | ||
| - | **[[2cqq]], [[2cqr]] - | + | **[[2cqq]], [[2cqr]] - hDnaJC1 DNA-binding domain - NMR<br /> |
*DnaJ homolog subfamily C member 2 | *DnaJ homolog subfamily C member 2 | ||
| - | **[[2m2e]] - | + | **[[2m2e]] - hDnaJC2 SANT 2 domain - NMR<br /> |
*DnaJ homolog subfamily C member 3 | *DnaJ homolog subfamily C member 3 | ||
| - | **[[2y4t]], [[2y4u]] - | + | **[[2y4t]], [[2y4u]] - hDnaJC3 residues 35-461 <br /> |
| - | **[[3ieg]] - | + | **[[3ieg]] - mDnaJC3 TPR domain <br /> |
*DnaJ homolog subfamily C member 5 | *DnaJ homolog subfamily C member 5 | ||
| - | **[[2ctw]] - | + | **[[2ctw]] - DnaJC5 J domain - mouse - NMR<br /> |
| - | **[[2n04]], [[2n05]] - | + | **[[2n04]], [[2n05]] - hDnaJC5 N terminal domain - NMR<br /> |
*DnaJ homolog subfamily C member 10 | *DnaJ homolog subfamily C member 10 | ||
| - | **[[3apo]] - | + | **[[3apo]] - mDnaJC10 <br /> |
| - | **[[5ayk]], [[5ayl]] - | + | **[[5ayk]], [[5ayl]] - mDnaJC10 (mutant)<br /> |
| - | **[[3aps]] - | + | **[[3aps]] - hDnaJC10 TRX4 domain <br /> |
| - | **[[3apq]] - | + | **[[3apq]] - mDnaJC10 TRX4 domain <br /> |
*DnaJ homolog subfamily C member 24 | *DnaJ homolog subfamily C member 24 | ||
| - | **[[2l6l]] - | + | **[[2l6l]] - hDnaJC24 - NMR<br /> |
*DnaJ homolog DnJ-2 | *DnaJ homolog DnJ-2 | ||
| - | **[[2qsa]] - DnaJ J domain - ''Caenorhabditis elegans''<br /> | + | **[[2qsa]] - DnaJ-2 J domain - ''Caenorhabditis elegans''<br /> |
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:22, 1 November 2018
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3D structures of DnaJ homolog
Updated on 01-November-2018
References
- ↑ Terada K, Mori M. Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. J Biol Chem. 2000 Aug 11;275(32):24728-34. PMID:10816573 doi:http://dx.doi.org/10.1074/jbc.M002021200
- ↑ Rauch JN, Gestwicki JE. Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. J Biol Chem. 2014 Jan 17;289(3):1402-14. doi: 10.1074/jbc.M113.521997. Epub 2013 , Dec 5. PMID:24318877 doi:http://dx.doi.org/10.1074/jbc.M113.521997
- ↑ Stark JL, Mehla K, Chaika N, Acton TB, Xiao R, Singh PK, Montelione GT, Powers R. Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer. Biochemistry. 2014 Mar 4;53(8):1360-72. doi: 10.1021/bi401329a. Epub 2014 Feb 19. PMID:24512202 doi:http://dx.doi.org/10.1021/bi401329a
