Φ29 DNA polymerase residues Tyr59, His61 and Phe69 of the highly conserved Exoll motif are essential for interaction with the terminal protein

Nucleic Acids Research

Volumn 30, Issue 6, 2002, Pages 1379-1386

  Eisenbrandt, Ralf ^a   Lázaro, José M ^a   Salas, Margarita ^a   de Vega, Miguel ^a  

^a UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DNA; DNA POLYMERASE; HISTIDINE; PHENYLALANINE; PRIMER DNA; PROTEIN; TYROSINE; DEOXYADENOSINE PHOSPHATE; DNA DIRECTED DNA POLYMERASE; P3 PROTEIN, BACTERIOPHAGE PHI 29; VIRUS PROTEIN;

ARTICLE; CONTROLLED STUDY; DNA REPLICATION; DNA SYNTHESIS; GENE MUTATION; GENETIC CONSERVATION; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; AMINO ACID SEQUENCE; BACTERIOPHAGE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

EUKARYOTA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIOPHAGES; CATALYTIC DOMAIN; CONSERVED SEQUENCE; DEOXYADENINE NUCLEOTIDES; DNA; DNA REPLICATION; DNA-DIRECTED DNA POLYMERASE; HISTIDINE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; SEQUENCE ALIGNMENT; TYROSINE; VIRAL PROTEINS;

EID: 0037085567     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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