Loss of polymerase activity due to Tyr to Phe substitution in the YMDD motif of human immunodeficiency virus type-1 reverse transcriptase is compensated by met to val substitution within the same motif

Biochemistry

Volumn 37, Issue 27, 1998, Pages 9630-9640

  Harris, Dylan ^a   Yadav, Prem N S ^a   Pandey, Virendra N ^a  

^a RUTGERS NEW JERSEY MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; METHIONINE; MUTANT PROTEIN; PHENYLALANINE; RNA DIRECTED DNA POLYMERASE; TYROSINE; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; DNA SYNTHESIS; DNA TEMPLATE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; PRIORITY JOURNAL; VIRUS GENE;

AMINO ACID SUBSTITUTION; BASE SEQUENCE; DEOXYRIBONUCLEOTIDES; DIDEOXYNUCLEOSIDES; DNA, VIRAL; DNA-DIRECTED DNA POLYMERASE; ENZYME ACTIVATION; HIV-1 REVERSE TRANSCRIPTASE; HUMANS; KINETICS; METHIONINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEOCAPSID PROTEINS; PHENYLALANINE; RNA, VIRAL; SUBSTRATE SPECIFICITY; TEMPLATES, GENETIC; TYROSINE; VALINE;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0032493413     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi980549z     Document Type: Article

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