Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex. Academic Article uri icon

Overview

MeSH

  • Amino Acid Sequence
  • Base Composition
  • Base Sequence
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Conformation
  • Protein Structure, Secondary

MeSH Major

  • Gene Products, tat
  • Immunodeficiency Virus, Bovine
  • RNA, Viral

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.

publication date

  • November 17, 1995

has subject area

  • Amino Acid Sequence
  • Base Composition
  • Base Sequence
  • Gene Products, tat
  • Hydrogen Bonding
  • Immunodeficiency Virus, Bovine
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Conformation
  • Protein Structure, Secondary
  • RNA, Viral

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed ID

  • 7502045

Additional Document Info

start page

  • 1200

end page

  • 1203

volume

  • 270

number

  • 5239