Molecular Playground/DnaK: Difference between revisions
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<scene name='60/609794/Adp-dnak_1/4'>DnaK in the extended conformation</scene> | <scene name='60/609794/Adp-dnak_1/4'>DnaK in the extended conformation</scene> | ||
The <i>E. coli</i> Hsp70, DnaK, is a protein chaperone whose function is to bind exposed hydrohpobic residues of unfolded proteins. This binding event prevents aggregation and rescues the nascent chain from kinetic traps along the folding pathway. Hsp70 protein chaperones switch between an <scene name='60/609794/Atp-dnak/1'>ATP-bound</scene>, low-substrate affinity form and an <scene name='60/609794/Adp-dnak_1/4'>ADP-bound</scene>, high substrate affinity form during their allosteric cycle.[http://www.ncbi.nlm.nih.gov/pubmed/19439666?dopt=Abstract 1] Hsp70 protein chaperones are ubiquitously found in almost all known organisms and cell types and represent a potential target for anti-cancer and neurodegenerative therapies.[http://www.ncbi.nlm.nih.gov/pubmed/21403392 2] | The <i>E. coli</i> '''Hsp70''', '''DnaK''', is a protein chaperone whose function is to bind exposed hydrohpobic residues of unfolded proteins. This binding event prevents aggregation and rescues the nascent chain from kinetic traps along the folding pathway. Hsp70 protein chaperones switch between an <scene name='60/609794/Atp-dnak/1'>ATP-bound</scene>, low-substrate affinity form and an <scene name='60/609794/Adp-dnak_1/4'>ADP-bound</scene>, high substrate affinity form during their allosteric cycle.[http://www.ncbi.nlm.nih.gov/pubmed/19439666?dopt=Abstract 1] Hsp70 protein chaperones are ubiquitously found in almost all known organisms and cell types and represent a potential target for anti-cancer and neurodegenerative therapies.[http://www.ncbi.nlm.nih.gov/pubmed/21403392 2] | ||
===Structure=== | ===Structure=== | ||
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===3D structures of Hsp70=== | ===3D structures of Hsp70=== | ||
[[Heat Shock Proteins]] | |||
===See Also=== | ===See Also=== | ||
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===References=== | ===References=== | ||
1. Bertelsen EB. et al. Proc Natl Acad Sci USA 2009 | 1. [http://www.ncbi.nlm.nih.gov/pubmed/19439666?dopt=Abstract Bertelsen EB. et al. Proc Natl Acad Sci USA 2009] | ||
2. Broer L. et al. J Alzherimers Dis 2011 | 2. [http://www.ncbi.nlm.nih.gov/pubmed/21403392 Broer L. et al. J Alzherimers Dis 2011] | ||
3. Zuiderweg ER. et al. Top Curr Chem 2013 | 3. [http://www.ncbi.nlm.nih.gov/pubmed/22576356 Zuiderweg ER. et al. Top Curr Chem 2013] | ||
4. Wegele H. et al. Rev Physiol Biochem Pharmacol 2004 | 4. [http://www.ncbi.nlm.nih.gov/pubmed/14740253 Wegele H. et al. Rev Physiol Biochem Pharmacol 2004] | ||
5. Zhuravleva A. et al. Proc Natl Acad Sci USA 2011 | 5. [http://www.ncbi.nlm.nih.gov/pubmed/21482798 Zhuravleva A. et al. Proc Natl Acad Sci USA 2011] | ||
6. | 6. [http://www.ncbi.nlm.nih.gov/pubmed/17434124?dopt=Abstract Swain JF. et al. Mol Cell 2007] | ||
7. | 7. [http://www.ncbi.nlm.nih.gov/pubmed/23123194?dopt=Abstract Kityk, R. et al. Mol Cell 2012] | ||
8. Mayer MP. Trends Biochem Sci 2013 | 8. [http://www.ncbi.nlm.nih.gov/pubmed/24012426 Mayer MP. Trends Biochem Sci 2013] | ||
9. Sharma SK. et al. Nat Chem Bio 2010 | 9. [http://www.ncbi.nlm.nih.gov/pubmed/20953191 Sharma SK. et al. Nat Chem Bio 2010] | ||
10. Zhuravleva A. et al. Cell 2012 | 10. [http://www.ncbi.nlm.nih.gov/pubmed/23217711 Zhuravleva A. et al. Cell 2012] | ||
11. Li X. et al. ACS Med Chem Lett 2013 | 11. [http://www.ncbi.nlm.nih.gov/pubmed/24312699 Li X. et al. ACS Med Chem Lett 2013] | ||
12. [http://www.ncbi.nlm.nih.gov/pubmed/22920901 Assimon VA. et al. Curr Pharm Des 2013] | 12. [http://www.ncbi.nlm.nih.gov/pubmed/22920901 Assimon VA. et al. Curr Pharm Des 2013] | ||
15. [http://www.ncbi.nlm.nih.gov/pubmed/22509487 Powers ET. et al. Cell Rep 2012] | 15. [http://www.ncbi.nlm.nih.gov/pubmed/22509487 Powers ET. et al. Cell Rep 2012] | ||