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

• Main Authors: Homouz, Dirar, Tan, Joyce Kwee Hong, Shamsir, Mohd. Shahir, Moustafa, Ibrahim M., Idriss, Haitham T.
• Format: Article
• Published: Elsevier Inc. 2018
• Subjects: QH301 Biology; TP Chemical technology
• Online Access: http://eprints.utm.my/id/eprint/85466/; http://dx.doi.org/10.1016/j.jmgm.2018.08.007
• Institution: Universiti Teknologi Malaysia

DNA polymerase β 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...