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1996-02-27
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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).