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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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Detalhes bibliográficos
Publicado no:Biochemistry
Main Authors: Batra, Vinod K., Alnajjar, Khadijeh S., Sweasy, Joann B., McKenna, Charles E., Goodman, Myron F., Wilson, Samuel H.
Formato: Artigo
Idioma:Inglês
Publicado em: 2020
Assuntos:
Acesso em linha: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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