Document 0364
 DOCN  M9490364
 TI    NMR structure of a biologically active peptide containing the
       RNA-binding domain of human immunodeficiency virus type 1 Tat.
 DT    9411
 AU    Mujeeb A; Bishop K; Peterlin BM; Turck C; Parslow TG; James TL;
       Department of Pharmaceutical Chemistry, University of California,; San
       Francisco 94143.
 SO    Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):8248-52. Unique Identifier
       : AIDSLINE MED/94336723
 AB    The Tat protein of human immunodeficiency virus type 1 enhances
       transcription by binding to a specific RNA element on nascent viral
       transcripts. Binding is mediated by a 10-amino acid basic domain that is
       rich in arginines and lysines. Here we report the three-dimensional
       peptide backbone structure of a biologically active 25-mer peptide that
       contains the human immunodeficiency virus type 1 Tat basic domain linked
       to the core regulatory domain of another lentiviral Tat--i.e., that from
       equine infectious anemia virus. Circular dichroism and two-dimensional
       proton NMR studies of this hybrid peptide indicate that the Tat basic
       domain forms a stable alpha-helix, whereas the adjacent regulatory
       sequence is mostly in extended form. These findings suggest that the
       tendency to form stable alpha-helices may be a common property of
       arginine- and lysine-rich RNA-binding domains.
 DE    Amino Acid Sequence  Binding Sites  Circular Dichroism  Gene Products,
       tat/*CHEMISTRY/*METABOLISM  HIV-1/*METABOLISM  Models, Structural
       Molecular Sequence Data  Nuclear Magnetic Resonance/METHODS  Peptide
       Fragments/*CHEMISTRY/*METABOLISM  *Protein Conformation  RNA,
       Viral/*METABOLISM  Software  Support, Non-U.S. Gov't  Support, U.S.
       Gov't, P.H.S.  Transcription, Genetic  JOURNAL ARTICLE

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