Skip NavigationSkip to Content
Return Return to Search Results

Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA : DNA

  1. Author:
    Sarafianos, S. G.
    Das, K.
    Tantillo, C.
    Clark, A. D.
    Ding, J.
    Whitcomb, J. M.
    Boyer, P. L.
    Hughes, S. H.
    Arnold, E.

  2. Author Address

    Ctr Adv Biotechnol & Med, 679 Hoes Lane, Piscataway, NJ 08854 USA. Ctr Adv Biotechnol & Med, Piscataway, NJ 08854 USA. Rutgers State Univ, Dept Chem, Piscataway, NJ 08854 USA. ViroLog Inc, S San Francisco, CA 94080 USA. NCI, Frederick Canc Res & Dev Ctr, HIV D Resistance Program, Frederick, MD 21702 USA. Arnold E Ctr Adv Biotechnol & Med, 679 Hoes Lane, Piscataway, NJ 08854 USA.
    1. Year: 2001
  2. Journal: Embo Journal
    1. 20
    2. 6
    3. Pages: 1449-1461
  4. Type of Article: Article
  1. Abstract:

    We have determined the 3.0 Angstrom resolution structure of wild-type HIV-1 reverse transcriptase in complex with an RNA:DNA oligonucleotide whose sequence includes a purine-rich segment from the HIV-1 genome called the polypurine tract (PPT). The PPT is resistant to ribonuclease H (RNase H) cleavage and is used as a primer for second DNA strand synthesis. The 'RNase H primer grip', consisting of amino acids that interact with the DNA primer strand, may contribute to PNase H catalysis and cleavage specificity. Cleavage specificity is also controlled by the width of the minor groove and the trajectory of the RNA:DNA, both of which are sequence dependent, An unusual 'unzipping' of 7 bp occurs in the adenine stretch of the PPT: an unpaired base on the template strand takes the base pairing out of register and then, following two offset base pairs, an unpaired base on the primer strand re- establishes the normal register. The structural aberration extends to the RNase H active site and may play a role in the resistance of PPT to RNase H cleavage.

    See More

  1. Keywords:

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel