Threonine 79 is a hinge residue that governs the fidelity of DNA polymerase β by helping to position the DNA within the active site

Journal of Biological Chemistry

Volumn 277, Issue 38, 2002, Pages 35550-35560

  Maitra, Mausumi ^a,b,c,d,e   Gudzelak Jr , Andrew ^a,b,c,d,e   Li, Shu Xia ^a,b,c,d,e   Matsumoto, Yoshihiro ^a,b,c,d,e   Eckert, Kristin A ^a,b,c,d,e   Jager, Joachim ^a,b,c,d,e   Sweasy, Joann B ^a,b,c,d,e  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b PENN STATE CANCER INSTITUTE   (United States)

^c FOX CHASE CANCER CENTER   (United States)

^d UNIVERSITY OF LEEDS   (United Kingdom)

^e CURAGEN CORPORATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOASSAY; CATALYSIS; ENZYMES; GENETIC ENGINEERING; HYDROGEN BONDS;

GENETIC SCREEN;

DNA;

AMINO ACID; DNA DIRECTED DNA POLYMERASE BETA; THREONINE;

AMINO TERMINAL SEQUENCE; ARTICLE; DNA STRUCTURE; DNA SYNTHESIS; DNA TEMPLATE; ENZYME ACTIVE SITE; ENZYME ASSAY; GENETIC SCREENING; HERPES SIMPLEX VIRUS 1; HYDROGEN BOND; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN MOTIF;

BASE SEQUENCE; BINDING SITES; DNA POLYMERASE BETA; DNA PRIMERS; DNA REPLICATION; DNA, BACTERIAL; FRAMESHIFT MUTATION; PHENOTYPE; THREONINE;

HUMAN HERPESVIRUS 1; SIMPLEXVIRUS;

EID: 0037144446     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M204953200     Document Type: Article

References (43)