Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1999-9-3
pubmed:abstractText
Basic peptides from the carboxy terminus of the HIV-1 Tat protein bind to the apical stem-loop region of TAR RNA with high affinity and moderate specificity. The conformations of the unbound and 24 residue Tat peptide (Tfr24)-bound forms of TAR RNA have been characterized by NMR spectroscopy. The unbound form of TAR exists in major and minor forms having different trinucleotide bulge conformations. A specific TAR RNA conformational change is observed upon complex formation with Tfr24, consisting of coaxial stacking of helical stems and base triple formation. A U23-A27-U38 base triple is proposed based on exchangeable proton NMR data, where U23 forms a base pair with A27 in the major groove. No evidence for base triple formation was found for Tat peptides in which lysine residues are extensively substituted for arginine.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10059-69
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:10433713-Amino Acid Sequence, pubmed-meshheading:10433713-Base Composition, pubmed-meshheading:10433713-Gene Products, tat, pubmed-meshheading:10433713-HIV Long Terminal Repeat, pubmed-meshheading:10433713-HIV-1, pubmed-meshheading:10433713-Humans, pubmed-meshheading:10433713-Hydrogen Bonding, pubmed-meshheading:10433713-Models, Chemical, pubmed-meshheading:10433713-Models, Molecular, pubmed-meshheading:10433713-Molecular Sequence Data, pubmed-meshheading:10433713-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:10433713-Nucleic Acid Conformation, pubmed-meshheading:10433713-Peptide Fragments, pubmed-meshheading:10433713-Protein Binding, pubmed-meshheading:10433713-Protein Conformation, pubmed-meshheading:10433713-RNA, Viral, pubmed-meshheading:10433713-Solutions, pubmed-meshheading:10433713-tat Gene Products, Human Immunodeficiency Virus
pubmed:year
1999
pubmed:articleTitle
Characterization of the solution conformations of unbound and Tat peptide-bound forms of HIV-1 TAR RNA.
pubmed:affiliation
Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.