Document Detail


Aqueous solution structure of a hybrid lentiviral Tat peptide and a model of its interaction with HIV-1 TAR RNA.
MedLine Citation:
PMID:  8906885     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human immunodeficiency virus, type 1, (HIV-1) encodes a transactivating regulatory protein, called Tat, which is required for efficient transcription of the viral genome. Tat acts by binding to a specific RNA stem-loop element, called TAR, on nascent viral transcripts. The specificity of binding is principally determined by residues in a short, highly basic domain of Tat. The structure in aqueous solution of a biologically active peptide, comprised of the ten-amino acid HIV-1 Tat basic domain linked to a 15-amino acid segment of the core regulatory domain of another lentiviral Tat, i.e., that from equine infectious anemia virus (EIAV), has been determined. The restraint data set includes interproton distance bounds determined from two-dimensional nuclear Overhauser effect (2D NOE) spectra via a complete relaxation matrix analysis. Thirty structures consistent with the experimental data were generated via the distance geometry program DIANA. Subsequent restrained molecular mechanics calculations were used to define the conformational space subtended by the peptide. A large fraction of the 25-mer peptide assumes a structure in aqueous solution with the lysine- and arginine-rich HIV-1 basic domain being separated from the basic domain by a turn and characterized by a nascent helix as well. The Tat peptide/TAR complex could be modeled with the basic alpha-helix lying in the major groove of TAR such that important interactions of a putative specificity-endowing arginine are maintained and very slight widening of the major groove is entailed.
Authors:
A Mujeeb; T G Parslow; Y C Yuan; T L James
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of biomolecular structure & dynamics     Volume:  13     ISSN:  0739-1102     ISO Abbreviation:  J. Biomol. Struct. Dyn.     Publication Date:  1996 Feb 
Date Detail:
Created Date:  1997-04-30     Completed Date:  1997-04-30     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  8404176     Medline TA:  J Biomol Struct Dyn     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  649-60     Citation Subset:  IM; X    
Affiliation:
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Gene Products, tat / chemical synthesis,  chemistry*,  metabolism
HIV Long Terminal Repeat / physiology*
HIV-1 / genetics,  metabolism*
Humans
Infectious Anemia Virus, Equine / chemistry
Magnetic Resonance Spectroscopy
Mathematical Computing*
Models, Molecular*
Molecular Sequence Data
Protein Structure, Secondary
Sequence Homology, Amino Acid
Solutions
tat Gene Products, Human Immunodeficiency Virus
Grant Support
ID/Acronym/Agency:
AI29313/AI/NIAID NIH HHS; GM39247/GM/NIGMS NIH HHS; GM41639/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Gene Products, tat; 0/Solutions; 0/tat Gene Products, Human Immunodeficiency Virus

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