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Revealing an Internal Stabilization Deficiency in the DNA Polymerase β K289M Cancer Variant through the Combined Use of Chemical Biology and X-ray Crystallography

The human DNA polymerase (pol) β cancer variant K289M has altered polymerase activity in vitro, and the structure of wild-type pol β reveals that the K289 side chain contributes to a network of stabilizing interactions in a C-terminal region of the enzyme distal to the active site. Here, we probed t...

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Vydáno v:Biochemistry
Hlavní autoři: Batra, Vinod K., Alnajjar, Khadijeh S., Sweasy, Joann B., McKenna, Charles E., Goodman, Myron F., Wilson, Samuel H.
Médium: Artigo
Jazyk:Inglês
Vydáno: 2020
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC7263314/
https://ncbi.nlm.nih.gov/pubmed/31999437
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.9b01072
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