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Analysis of the Structure of Chemically Synthesized Hiv-1 Protease Complexed With a Hexapeptide Inhibitor .1. Crystallographic Refinement of 2 Angstrom Data

  1. Author:
    Miller, M.
    Geller, M.
    Gribskov, M.
    Kent, S. B. H.

  2. Author Address

    Miller M NCI FREDERICK CANC RES FACIL & DEV CTR MACROMOL STRUCT LAB POB B FREDERICK, MD 21702 USA NCI FREDERICK CANC RES FACIL & DEV CTR MATH BIOL LAB FREDERICK, MD 21701 USA UNIV WARSAW INST EXPT PHYS DEPT BIOPHYS WARSAW POLAND SCRIPPS CLIN & RES INST LA JOLLA, CA USA
    1. Year: 1997
  2. Journal: Proteins
    1. 27
    2. 2
    3. Pages: 184-194
  4. Type of Article: Article
  1. Abstract:

    The structure of a complex between a hexapeptide-based inhibitor, MVT-101, and the chemically synthesized (Aba 67,95,167,195; Aba: L-alpha-amino-butyric acid) protease from the human immunodeficiency virus (HIV-1), reported previously at 2.3 Angstrom has now been refined to a crystallographic R factor of 15.4% at 2.0 Angstrom resolution, Root mean square deviations from ideality are 0.18 Angstrom for bond lengths and 2.4 degrees for the angles, The inhibitor can be fitted to the difference electron density map in two alternative orientations, Drastic differences are observed for positions and interactions at P3/S3 and P3'/S3' subsites of the two orientations due to different crystallographic environments. (C) 1997 Wiley-Liss, Inc. [References: 39]

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