Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics

Internal cavities are a common feature of many proteins, often having profound effects on the dynamics of their interactions with substrate and binding partners. RB69 DNA polymerase (pol) has a hydrophobic cavity right below the nucleotide binding pocket at the tip of highly conserved L415 side chai...

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Detalles Bibliográficos
Autores principales: Xia, Shuangluo, Wood, Marcus, Bradley, Michael J., De La Cruz, Enrique M., Konigsberg, William H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2013
Materias:
Nucleic Acid Enzymes
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3799440/
https://www.ncbi.nlm.nih.gov/pubmed/23921641
http://dx.doi.org/10.1093/nar/gkt674

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3799440/
https://www.ncbi.nlm.nih.gov/pubmed/23921641
http://dx.doi.org/10.1093/nar/gkt674

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