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Article

Structure/function studies of human immunodeficiency virus type 1 reverse transcriptase. Alanine scanning mutagenesis of an alpha-helix in the thumb subdomain.

1 Nov 1994

Abstract excerpt

Human immunodeficiency virus type 1 reverse transcriptase has subunits of 66 and 51 kDa (p66 and p51, respectively). Structural studies indicate that each subunit consists of common subdomains. The polymerase domain of p66 forms a nucleic acid binding cleft, and, by analogy with a right hand, the subdomains are referred to as fingers, palm, and thumb (Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A., and...

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Identifiers

PMID: 7525566
DOI: 10.1016/s0021-9258(18)46899-8

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Structure/function studies of human immunodeficiency virus type 1 reverse transcriptase. Alanine scanning mutagenesis of an alpha-helix in the thumb subdomain.PMID 7525566Read ↗

Alterations to the primer grip of p66 HIV-1 reverse transcriptase and their consequences for template-primer utilization.Semantic proximity Read ↗

Analysis of amino acids in the beta7-beta8 loop of human immunodeficiency virus type 1 reverse transcriptase for their role in virus replication.Semantic proximity Read ↗

Mutational analysis of the fingers and palm subdomains of human immunodeficiency virus type-1 (HIV-1) reverse transcriptase.Semantic proximity Read ↗

Kinetic analysis of four HIV-1 reverse transcriptase enzymes mutated in the primer grip region of p66. Implications for DNA synthesis and dimerization.Semantic proximity Read ↗

Mutational sensitivity patterns define critical residues in the palm subdomain of the reverse transcriptase of human immunodeficiency virus type 1.Semantic proximity Read ↗

Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase.Semantic proximity Read ↗

Substitutions of Phe61 located in the vicinity of template 5'-overhang influence polymerase fidelity and nucleoside analog sensitivity of HIV-1 reverse transcriptase.Semantic proximity Read ↗

Relationship between enzyme activity and dimeric structure of recombinant HIV-1 reverse transcriptase.Semantic proximity Read ↗

Residues in the alphaH and alphaI helices of the HIV-1 reverse transcriptase thumb subdomain required for the specificity of RNase H-catalyzed removal of the polypurine tract primer.Semantic proximity Read ↗

Identification of amino acid residues in the human immunodeficiency virus type-1 reverse transcriptase tryptophan-repeat motif that are required for subunit interaction using infectious virions.Semantic proximity Read ↗

Mutating a Conserved Motif of the HIV-1 Reverse Transcriptase Palm Subdomain Alters Primer UtilizationSemantic proximity Read ↗

Insertion of a small peptide of six amino acids into the beta7-beta8 loop of the p51 subunit of HIV-1 reverse transcriptase perturbs the heterodimer and affects its activities.Semantic proximity Read ↗

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