Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches

Journal of Virology

Volumn 75, Issue 11, 2001, Pages 4990-4998

  Bridges, Kristie Grove ^a,b   Chow, Connie S ^a,c   Coen, Donald M ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b PFIZER INC   (United States)

^c HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; VIRUS PROTEIN;

ANTIVIRAL ACTIVITY; ARTICLE; BAY REGION BINDING SITE; CALORIMETRY; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; DNA SYNTHESIS; ENTHALPY; ENZYME SUBUNIT; GENE MUTATION; GENETIC ENGINEERING; HERPES SIMPLEX VIRUS; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; TITRIMETRY; VIRUS REPLICATION;

ALANINE; AMINO ACID SUBSTITUTION; CALORIMETRY, DIFFERENTIAL SCANNING; DNA-DIRECTED DNA POLYMERASE; EXODEOXYRIBONUCLEASES; GLUTAMINE; HYDROGEN BONDING; LIGANDS; MUTATION; PEPTIDES; PROTEIN BINDING; SEQUENCE ALIGNMENT; SIMPLEXVIRUS; VIRAL PROTEINS; VIRUS REPLICATION;

EID: 0035038393     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.75.11.4990-4998.2001     Document Type: Article

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