Molecular chaperones: clasping the prize
- PMID: 8994816
- DOI: 10.1016/s0960-9822(02)70775-6
Molecular chaperones: clasping the prize
Abstract
The three-dimensional structure of the substrate-binding domain of DnaK, a bacterial Hsp70, shows how such molecular chaperones can be so promiscuous in recognizing different proteins, yet so accurate in discriminating between unfolded and folded forms of their polypeptide substrates.
Similar articles
-
Structural insights into substrate binding by the molecular chaperone DnaK.Nat Struct Biol. 2000 Apr;7(4):298-303. doi: 10.1038/74062. Nat Struct Biol. 2000. PMID: 10742174
-
Interdomain communication in the molecular chaperone DnaK.Biochem J. 2003 Feb 1;369(Pt 3):627-34. doi: 10.1042/BJ20020943. Biochem J. 2003. PMID: 12383055 Free PMC article.
-
Conformational properties of bacterial DnaK and yeast mitochondrial Hsp70. Role of the divergent C-terminal alpha-helical subdomain.FEBS J. 2005 Jun;272(12):3184-96. doi: 10.1111/j.1742-4658.2005.04737.x. FEBS J. 2005. PMID: 15955075
-
The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?Mol Microbiol. 2002 Sep;45(5):1197-206. doi: 10.1046/j.1365-2958.2002.03093.x. Mol Microbiol. 2002. PMID: 12207689 Review.
-
Hsp70 chaperones: cellular functions and molecular mechanism.Cell Mol Life Sci. 2005 Mar;62(6):670-84. doi: 10.1007/s00018-004-4464-6. Cell Mol Life Sci. 2005. PMID: 15770419 Free PMC article. Review.
Cited by
-
Huntington's Disease.Cold Spring Harb Perspect Biol. 2011 Jun 1;3(6):a007476. doi: 10.1101/cshperspect.a007476. Cold Spring Harb Perspect Biol. 2011. PMID: 21441583 Free PMC article. Review.
-
Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophys Chem. 2022 Aug;287:106821. doi: 10.1016/j.bpc.2022.106821. Epub 2022 Apr 29. Biophys Chem. 2022. PMID: 35667131 Free PMC article. Review.
-
Enhanced measles virus cDNA rescue and gene expression after heat shock.J Virol. 1999 May;73(5):3560-6. doi: 10.1128/JVI.73.5.3560-3566.1999. J Virol. 1999. PMID: 10196245 Free PMC article.
-
The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response.Arch Toxicol. 2021 Jun;95(6):1943-1970. doi: 10.1007/s00204-021-03070-8. Epub 2021 May 18. Arch Toxicol. 2021. PMID: 34003342 Review.
-
Amorphous protein aggregates stimulate plasminogen activation, leading to release of cytotoxic fragments that are clients for extracellular chaperones.J Biol Chem. 2017 Sep 1;292(35):14425-14437. doi: 10.1074/jbc.M117.786657. Epub 2017 Jul 14. J Biol Chem. 2017. PMID: 28710283 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources