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Structure of the unbound form of HIV-1 subtype A protease: comparison with unbound forms of proteases from other HIV subtypes

  1. Author:
    Robbins, A. H.
    Coman, R. M.
    Bracho-Sanchez, E.
    Fernandez, M. A.
    Gilliland, C. T.
    Li, M.
    Agbandje-McKenna, M.
    Wlodawer, A.
    Dunn, B. M.
    McKenna, R.

  2. Author Address

    [Robbins, Arthur H.; Coman, Roxana M.; Bracho-Sanchez, Edith; Fernandez, Marty A.; Gilliland, C. Taylor; Agbandje-McKenna, Mavis; Dunn, Ben M.; McKenna, Robert] Univ Florida, Dept Biochem & Mol Biol, Gainesville, FL 32610 USA. [Li, Mi] SAIC Frederick, Basic Res Program, Frederick, MD USA. [Li, Mi; Wlodawer, Alexander] NCI, Macromol Crystallog Lab, Frederick, MD 21701 USA.;Dunn, BM, Univ Florida, Dept Biochem & Mol Biol, Gainesville, FL 32610 USA.;bdunn@ufl.edu rmckenna@ufl.edu
    1. Year: 2010
    2. Date: Mar
  2. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 66
    2. Pages: 233-242
  4. Type of Article: Article
  5. ISSN: 0907-4449
  1. Abstract:

    The crystal structure of the unbound form of HIV-1 subtype A protease (PR) has been determined to 1.7 angstrom resolution and refined as a homodimer in the hexagonal space group P6(1) to an R-cryst of 20.5%. The structure is similar in overall shape and fold to the previously determined subtype B, C and F PRs. The major differences lie in the conformation of the flap region. The flaps in the crystal structures of the unbound subtype B and C PRs, which were crystallized in tetragonal space groups, are either semi-open or wide open. In the present structure of subtype A PR the flaps are found in the closed position, a conformation that would be more anticipated in the structure of HIV protease complexed with an inhibitor. The amino-acid differences between the subtypes and their respective crystal space groups are discussed in terms of the differences in the flap conformations.

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External Sources

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  2. DOI: 10.1107/s0907444909054298
  3. View record in Web of Science®
  4. WOS: 000274536400002

Library Notes

  1. Fiscal Year: FY2009-2010
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