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Journal of Biological Inorganic Chemistry

Volumn 5, Issue 1, 2000, Pages 67-74

Metal-ion stoichiometry of the HIV-1 RT ribonuclease H domain: Evidence for two mutually exclusive sites leads to new mechanistic insights on metal- mediated hydrolysis in nucleic acid biochemistry

(6) Cowan, J A a Ohyama, Tsuyoshi a Howard, Kathryn b Rausch, Jason W c Cowan, Siu Man Lui a Le Grice, Stuart F J c

a OHIO STATE UNIVERSITY (United States)

b UNIVERSITY HOSPITALS OF CLEVELAND (United States)

c NATIONAL CANCER INSTITUTE (United States)

Author keywords

Calorimetry; Human immunodeficiency virus type 1 reverse transcriptase ribonuclease H domain; Mechanism; Metal binding; Stoichiometry

Indexed keywords

DIVALENT CATION; MAGNESIUM ION; MANGANESE; RIBONUCLEASE H; RNA DIRECTED DNA POLYMERASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROLYSIS; METAL BINDING; NONHUMAN; NUCLEIC ACID METABOLISM; PRIORITY JOURNAL; PROTEIN DOMAIN; REACTION ANALYSIS; STOICHIOMETRY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ESCHERICHIA COLI; HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0034002794 PISSN: 09498257 EISSN: None Source Type: Journal
DOI: 10.1007/s007750050009 Document Type: Article

Times cited : (50)

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