Cited by 316Enzyme Structure and FunctionHIV/AIDS drug development and treatmentProtein Structure and Dynamics

An open and closed case for all polymerases

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Doublié, Sylvie, Sawaya, Michael R, Ellenberger, Tom·1999·Structure

Abstract

The recently determined structures of HIV-1 reverse transcriptase and Taq DNA polymerase in complex with DNA primer-template and an incoming nucleotide have shown that a large conformational change configures the polymerase active site for nucleotidyl transfer. The structure of reverse transcriptase in the catalytic complex will open the path to the rational design of novel nucleoside analog inhibitors of viral replication.

Integrity signals

Registry

Crossref · 10.1016/s0969-2126(99)80017-3

Cites

24 of 24 references verified0 citation errors · 0 not checkable

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Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Crystal structures reveal that polymerase binding to DNA strongly reshapes the primer-template, for example the backbone at the templating base can be bent by 90°.

    “Crystal structures (Refs.15-22 and references therein) reveal that polymerase binding to DNA strongly reshapes the primertemplate, e.g. the backbone at the templating base can be bent by 90°.”

    From DNA Replication Fidelity (2004) · cites this paper as [18]

  • Polymerases in families A, B, X, and RT have nascent base pair binding pockets that tightly accommodate a correct Watson-Crick base pair.

    “Polymerases in families A, B, X, and RT have nascent base pair binding pockets that tightly accommodate a correct Watson-Crick base pair (Fig. 2A and additional images in Refs.15-19 and references therein).”

    From DNA Replication Fidelity (2004) · cites this paper as [18]

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Authors
Doublié, S., Sawaya, M. R., & Ellenberger, T.
Affiliations
  • University of Vermont (US)
  • Harvard University (US)
Corresponding author
Ellenberger, Tom
Venue
Structure
Publisher
Elsevier BV
Published
1999-02
Volume
7
Issue
2
Pages
R31-R35
ISSN
0969-2126 (ISSN-L)
OpenAlex
W2036894316
Cited by
314
References
24
Citations by year
2026: 4 · 2025: 4 · 2024: 8 · 2023: 5 · 2022: 6 · 2021: 7 · 2020: 6 · 2019: 4 · 2018: 6 · 2017: 11 · 2016: 9 · 2015: 8 · 2014: 19 · 2013: 13 · 2012: 8
FWCI
13.72
Type
journal article
Language
en
Open access
Locations
  • Structure (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institutes of Health
Topics
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
polymerase active site, HIV-1 reverse transcriptase, Taq DNA polymerase, nucleotidyl transfer, conformational change, primer-template complex, rational drug design, polymerase structure
MeSH terms
Binding Sites, DNA-Directed DNA Polymerase, Models, Molecular, HIV-1, Protein Structure, Secondary, DNA Primers, Taq Polymerase, HIV Reverse Transcriptase

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