       Document 0297
 DOCN  M9630297
 TI    Solution structure of a bovine immunodeficiency virus Tat-TAR
       peptide-RNA complex.
 DT    9603
 AU    Puglisi JD; Chen L; Blanchard S; Frankel AD; Department of Chemistry and
       Biochemistry, University of; California, Santa Cruz 95064, USA.
 SO    Science. 1995 Nov 17;270(5239):1200-3. Unique Identifier : AIDSLINE
       MED/96072972
 AB    The Tat protein of bovine immunodeficiency virus (BIV) binds to its
       target RNA, TAR, and activates transcription. A 14-amino acid
       arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat
       binds specifically to BIV TAR, and biochemical and in vivo experiments
       have identified the amino acids and nucleotides required for binding.
       The solution structure of the RNA-peptide complex has now been
       determined by nuclear magnetic resonance spectroscopy. TAR forms a
       virtually continuous A-form helix with two unstacked bulged nucleotides.
       The peptide adopts a beta-turn conformation and sits in the major groove
       of the RNA. Specific contacts are apparent between critical amino acids
       in the peptide and bases and phosphates in the RNA. The structure is
       consistent with all biochemical data and demonstrates ways in which
       proteins can recognize the major groove of RNA.
 DE    Amino Acid Sequence  Base Composition  Base Sequence  Gene Products,
       tat/*CHEMISTRY/METABOLISM  Hydrogen Bonding  Immunodeficiency Virus,
       Bovine/*CHEMISTRY  Models, Molecular  Molecular Sequence Data  Nuclear
       Magnetic Resonance  Nucleic Acid Conformation  Protein Conformation
       Protein Structure, Secondary  RNA, Viral/*CHEMISTRY/METABOLISM  Support,
       Non-U.S. Gov't  Support, U.S. Gov't, P.H.S.  JOURNAL ARTICLE

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

