Document 0165
 DOCN  M95A0165
 TI    High resolution structures of HIV-1 RT from four RT-inhibitor complexes.
 DT    9510
 AU    Ren J; Esnouf R; Garman E; Somers D; Ross C; Kirby I; Keeling J; Darby
       G; Jones Y; Stuart D; et al; Laboratory of Molecular Biophysics, Oxford,
       UK.
 SO    Nat Struct Biol. 1995 Apr;2(4):293-302. Unique Identifier : AIDSLINE
       MED/95316679
 AB    We have determined the structures of four complexes of HIV-1 reverse
       transcriptase with non-nucleoside inhibitors, three fully refined at
       high resolution. The highest resolution structure is of the
       RT-nevirapine complex which has an R-factor of 0.186 and a
       root-mean-square bond length deviation of 0.015 A for all data to 2.2 A.
       The structures reveal a common mode of binding for these chemically
       diverse compounds. The common features of binding are largely
       hydrophobic interactions and arise from induced shape complementarity
       achieved by conformational rearrangement of the enzyme and
       conformational/configurational rearrangement of the compounds.
 DE    Amino Acid Sequence  Antiviral Agents/CHEMISTRY/*METABOLISM  Binding
       Sites  Comparative Study  Computer Graphics  Crystallography, X-Ray
       Drug Design  HIV-1/ENZYMOLOGY  Models, Molecular  Molecular Sequence
       Data  Mutagenesis, Site-Directed  Point Mutation  *Protein Conformation
       Protein Structure, Secondary  Pyridines/CHEMISTRY/*METABOLISM
       Recombinant Proteins/ANTAGONISTS & INHIB/CHEMISTRY  Reverse
       Transcriptase/*ANTAGONISTS & INHIB/*CHEMISTRY  Support, Non-U.S. Gov't
       JOURNAL ARTICLE

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