Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance.

Science (New York, N.Y.) - 27 Nov 1998

Huang H, Chopra R, Verdine G L, Harrison S C

Abstract excerpt

A combinatorial disulfide cross-linking strategy was used to prepare a stalled complex of human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase with a DNA template:primer and a deoxynucleoside triphosphate (dNTP), and the crystal structure of the complex was determined at a resolution of 3.2 angstroms. The presence of a dideoxynucleotide at the 3'-primer terminus allows capture of a state in which the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to DNA Primers
Share to DNA, Viral

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Drug Resistance, Microbial

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 9831551
DOI: 10.1126/science.282.5394.1669

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance.PMID 9831551Read ↗

Trapping of a catalytic HIV reverse transcriptase·template:primer complex through a disulfide bondSemantic proximity Read ↗

Trapping HIV-1 Reverse Transcriptase Before and After Translocation on DNASemantic proximity Read ↗

Evolving understanding of HIV-1 reverse transcriptase structure, function, inhibition, and resistance.Semantic proximity Read ↗

Catalytically-active complex of HIV-1 integrase with a viral DNA substrate binds anti-integrase drugs.Semantic proximity Read ↗

Structure and Function of HIV-1 Reverse Transcriptase: Molecular Mechanisms of Polymerization and InhibitionSemantic proximity Read ↗

Structural Aspects of Drug Resistance and Inhibition of HIV-1 Reverse TranscriptaseSemantic proximity Read ↗

The structure of HIV‐1 reverse transcriptase complexed with an RNA pseudoknot inhibitorSemantic proximity Read ↗

Molecular insights into the mechanisms of HIV-1 reverse transcriptase resistance to nucleoside analogs.Semantic proximity Read ↗

Structure of HIV-1 RT/dsRNA initiation complex prior to nucleotide incorporationSemantic proximity Read ↗

Nucleotide analogue binding, catalysis and primer unblocking in the mechanisms of HIV-1 reverse transcriptase-mediated resistance to nucleoside analogues.Semantic proximity Read ↗

Insights into HIV-1 Reverse Transcriptase (RT) Inhibition and Drug Resistance from Thirty Years of Structural StudiesSemantic proximity Read ↗

Crystal engineering of HIV-1 reverse transcriptase for structure-based drug designSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.