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 E. coli 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] 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] | 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] 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] | ||
===Structure=== | ===Structure=== | ||
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https://www.youtube.com/watch?v=yQ3QUDj1Mv8 | https://www.youtube.com/watch?v=yQ3QUDj1Mv8 | ||
The Gierasch lab, in collaboration with the Powers lab at Scripps, has developed a computational model of the proteostasis network in E. coli called FoldEco.[http://www.ncbi.nlm.nih.gov/pubmed/22509487] A web version of FoldEco can be found here: | The Gierasch lab, in collaboration with the Powers lab at Scripps, has developed a computational model of the proteostasis network in <i>E. coli</i> called FoldEco.[http://www.ncbi.nlm.nih.gov/pubmed/22509487] A web version of FoldEco can be found here: | ||
http://foldeco.scripps.edu | http://foldeco.scripps.edu | ||