Molecular dynamics simulations suggest changes in electrostatic interactions as a potential mechanism through which serine phosphorylation inhibits DNA polymerase β activity
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...
Main Authors: | Homouz, Dirar, Tan, Joyce Kwee Hong, Shamsir, Mohd. Shahir, Moustafa, Ibrahim M., Idriss, Haitham T. |
---|---|
Format: | Article |
Published: |
Elsevier Inc.
2018
|
Subjects: |
Similar Items
-
Molecular dynamics simulations suggest changes in electrostatic interactions as a potential mechanism through which serine phosphorylation inhibits DNA Polymerase β’s activity
by: Homouz, D., et al.
Published: (2018) -
Structural Insights into Phosphorylation-Mediated Polymerase Function Loss for DNA Polymerase <i>β</i> Bound to Gapped DNA
by: Amit Srivastava, et al.
Published: (2023-05-01) -
Bioinformatics analysis and molecular cloning of an extracellular serine protease from acinetobacter baumannii
by: Lim, Aik Siang
Published: (2018) -
Comparison of computational tools for protein-protein interaction (PPI) mapping and analysis
by: Geok, Wei Leong, et al.
Published: (2013) -
Gender identification of mouse embryos using the polymerase chain reaction (PCR) technique
by: Abdullah, Ramli, et al.
Published: (2006)