Molecular dynamics simulations suggest changes in electrostatic interactions as a potential mechanism through which serine phosphorylation inhibits DNA Polymerase β’s activity

DNA polymerase ß is a 39 kDa enzyme that is a major component of Base Excision Repair in human cells. The enzyme comprises two major domains, a 31 kDa domain responsible for the polymerase activity and an 8 kDa domain, which bind ssDNA and has a deoxyribose phosphate (dRP) lyase activity. DNA polyme...

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Bibliographic Details
Main Authors: Homouz, D., Tan, K. H. Joyce, Shamsir, M. Shahir, Moustafa, I. M., Idriss, H. T.
Format: Article
Language:English
Published: Elsevier Inc. 2018
Subjects:
Online Access:http://eprints.utm.my/id/eprint/81810/1/DirarMohammadAlHomouz2018_MolecularDynamicsSimulationsSuggestChanges.pdf
http://eprints.utm.my/id/eprint/81810/
http://dx.doi.org/10.1016/j.jmgm.2018.08.007
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