The C-terminal region of translesion synthesis DNA polymerase η is partially unstructured and has high conformational flexibility
- Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242-1109, USA
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- National Institutes of Health (NIH)
- OSTI ID:
- 1478096
- Journal Information:
- Nucleic Acids Research, Vol. 46, Issue 4; ISSN 0305-1048
- Publisher:
- Oxford University Press
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
Structural and Kinetic Analysis of Miscoding Opposite the DNA Adduct 1,N6 -Ethenodeoxyadenosine by Human Translesion DNA Polymerase $η$
Structural and Kinetic Analysis of Nucleoside Triphosphate Incorporation Opposite an Abasic Site by Human Translesion DNA Polymerase η
Metal-ion dependence of the active-site conformation of the translesion DNA polymerase Dpo4 from Sulfolobus solfataricus
Journal Article
·
Mon May 16 00:00:00 EDT 2016
· Journal of Biological Chemistry
·
OSTI ID:1478096
+3 more
Structural and Kinetic Analysis of Nucleoside Triphosphate Incorporation Opposite an Abasic Site by Human Translesion DNA Polymerase η
Journal Article
·
Mon Feb 09 00:00:00 EST 2015
· Journal of Biological Chemistry
·
OSTI ID:1478096
+3 more
Metal-ion dependence of the active-site conformation of the translesion DNA polymerase Dpo4 from Sulfolobus solfataricus
Journal Article
·
Wed Jul 18 00:00:00 EDT 2012
· Acta Crystallogr. F
·
OSTI ID:1478096
+2 more