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Volumn 281, Issue 13, 2006, Pages 8697-8706

Site-directed mutations of T4 helicase loading protein (gp59) reveal multiple modes of DNA polymerase inhibition and the mechanism of unlocking by gp41 helicase

(3) Nelson, Scott W a,b Yang, Jingsong a,c Benkovic, Stephen J a

a PENNSYLVANIA STATE UNIVERSITY (United States)

b Jane Coffin Childs Memorial Fund for Medical Research

c GLAXOSMITHKLINE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; DNA; HYDROPHOBICITY; MUTAGENESIS; SUBSTRATES;

DNA REPLICATION; MUTANTS; POLYMERASE;

ENZYME INHIBITION;

BINDING PROTEIN; DNA BINDING PROTEIN; DNA POLYMERASE; EXONUCLEASE; GLYCOPROTEIN GP 41; MUTANT PROTEIN; PROTEIN Y122A; SINGLE STRANDED DNA; T4 HELICASE LOADING PROTEIN; UNCLASSIFIED DRUG; DNA DIRECTED DNA POLYMERASE; HELICASE; VIRUS DNA;

ARTICLE; BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SYNTHESIS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; BACTERIOPHAGE T4; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; DRUG ANTAGONISM; ENZYMOLOGY; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENETICS; METABOLISM; PHYSIOLOGY; SITE DIRECTED MUTAGENESIS;

BACTERIOPHAGE T4; DNA HELICASES; DNA, VIRAL; DNA-DIRECTED DNA POLYMERASE; FLUORESCENCE RESONANCE ENERGY TRANSFER; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION;

EID: 33646841347 PISSN: 00219258 EISSN: 1083351X Source Type: Journal
DOI: 10.1074/jbc.M512185200 Document Type: Article

Times cited : (14)

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