Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
Abstract

HIV integrase is the enzyme responsible for inserting the viral DNA into the host chromosome; it is essential for HIV replication. The crystal structure of the catalytically active core domain (residues 50 to 212) of HIV-1 integrase was determined at 2.5 Å resolution. The central feature of the structure is a five-stranded β sheet flanked by helical regions. The overall topology reveals that this domain of integrase belongs to a superfamily of polynucleotidyl transferases that includes ribonuclease H and the Holliday junction resolvase RuvC. The active site region is identified by the position of two of the conserved carboxylate residues essential for catalysis, which are located at similar positions in ribonuclease H. In the crystal, two molecules form a dimer with an extensive solvent-inaccessible interface of 1300 Å 2 per monomer.

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Authors 6
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  2. Alison B. Hickman (additional)
  3. Timothy M. Jenkins (additional)
  4. Alan Engelman (additional)
  5. Robert Craigie (additional)
  6. David R. Davies (additional)
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Dates
Type When
Created 18 years, 10 months ago (Oct. 5, 2006, 8:01 p.m.)
Deposited 1 year, 7 months ago (Jan. 14, 2024, 11:29 p.m.)
Indexed 1 hour, 30 minutes ago (Aug. 24, 2025, 7:05 p.m.)
Issued 30 years, 8 months ago (Dec. 23, 1994)
Published 30 years, 8 months ago (Dec. 23, 1994)
Published Print 30 years, 8 months ago (Dec. 23, 1994)
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@article{Dyda_1994, title={Crystal Structure of the Catalytic Domain of HIV-1 Integrase: Similarity to Other Polynucleotidyl Transferases}, volume={266}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.7801124}, DOI={10.1126/science.7801124}, number={5193}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Dyda, Fred and Hickman, Alison B. and Jenkins, Timothy M. and Engelman, Alan and Craigie, Robert and Davies, David R.}, year={1994}, month=dec, pages={1981–1986} }