Summary information and primary citation
- PDB-id
-
1mnb;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- viral protein-RNA
- Method
- NMR
- Summary
- Biv tat peptide (residues 68-81), NMR, minimized
average structure
- Reference
-
Puglisi JD, Chen L, Blanchard S, Frankel AD (1995):
"Solution
structure of a bovine immunodeficiency virus Tat-TAR
peptide-RNA complex." Science,
270, 1200-1203.
- Abstract
- 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.
