Document 0459
 DOCN  M9460459
 TI    Identification of temperature-sensitive mutants of the human
       immunodeficiency virus type 1 protease through saturation mutagenesis.
       Amino acid side chain requirements for temperature sensitivity.
 DT    9404
 AU    Manchester M; Everitt L; Loeb DD; Hutchison CA 3rd; Swanstrom R;
       University of North Carolina, Lineberger Comprehensive Cancer; Center,
       Chapel Hill 27599.
 SO    J Biol Chem. 1994 Mar 11;269(10):7689-95. Unique Identifier : AIDSLINE
       MED/94171804
 AB    Human immunodeficiency virus type 1 encodes a protease whose activity is
       required for the production of infectious virus. An Escherichia coli
       expression and processing assay system was used to screen 285 protease
       mutants for temperature-sensitive activity. Fourteen protease mutants
       had a temperature-sensitive phenotype, and approximately half resulted
       from conservative amino acid substitutions. Of the 14 substitutions that
       conferred a temperature-sensitive phenotype, 11 substitutions occurred
       at 6 positions that represent 3 pairs of residues in the protease that
       contact each other in the three-dimensional structure. These mutants
       assist in pinpointing regions of the protease that are important for
       enzyme activity and stability.
 DE    Amino Acids/*METABOLISM  Enzyme Stability  HIV
       Protease/*GENETICS/METABOLISM  Models, Molecular  *Mutagenesis
       Phenotype  Protein Conformation  Support, U.S. Gov't, P.H.S.
       Temperature  JOURNAL ARTICLE

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