Document 0477
 DOCN  M9440477
 TI    Secondary structure and signal assignments of
       human-immunodeficiency-virus-1 protease complexed to a novel,
       structure-based inhibitor.
 DT    9404
 AU    Yamazaki T; Nicholson LK; Torchia DA; Stahl SJ; Kaufman JD; Wingfield
       PT; Domaille PJ; Campbell-Burk S; Bone Research Branch, National
       Institute of Dental Research, NIH,; Bethesda, MD 20892.
 SO    Eur J Biochem. 1994 Jan 15;219(1-2):707-12. Unique Identifier : AIDSLINE
       MED/94139754
 AB    We report comprehensive NMR studies in solution of the
       human-immunodeficiency-virus (HIV)-1 protease. Stable solutions of the
       protease were obtained by complexing the protein to a designed cyclic
       urea inhibitor DMP 323. A variety of triple-resonance experiments
       provided essentially complete 1H, 13C and 15N NMR signal assignments of
       the protease. These assignments, together with short-range NOE
       constraints, coupling constants and hydrogen-exchange data, yielded the
       secondary structure of the protease in solution. The results reported
       herein open the way to the determination of the high-resolution
       three-dimensional solution structures of protease/inhibitor complexes,
       as well as to studies of protease dynamics and solvent interactions.
 DE    Amino Acid Sequence  Cloning, Molecular  Escherichia coli  HIV
       Protease/*CHEMISTRY/*METABOLISM  HIV Protease Inhibitors/*METABOLISM
       Molecular Sequence Data  Mutagenesis, Site-Directed  Nuclear Magnetic
       Resonance/METHODS  Point Mutation  Protein Binding  *Protein Structure,
       Secondary  Recombinant Proteins/CHEMISTRY/METABOLISM  Support, U.S.
       Gov't, P.H.S.  Urea/*ANALOGS & DERIVATIVES/METABOLISM  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).