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M9490364.TXT
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1994-09-19
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Document 0364
DOCN M9490364
TI NMR structure of a biologically active peptide containing the
RNA-binding domain of human immunodeficiency virus type 1 Tat.
DT 9411
AU Mujeeb A; Bishop K; Peterlin BM; Turck C; Parslow TG; James TL;
Department of Pharmaceutical Chemistry, University of California,; San
Francisco 94143.
SO Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):8248-52. Unique Identifier
: AIDSLINE MED/94336723
AB The Tat protein of human immunodeficiency virus type 1 enhances
transcription by binding to a specific RNA element on nascent viral
transcripts. Binding is mediated by a 10-amino acid basic domain that is
rich in arginines and lysines. Here we report the three-dimensional
peptide backbone structure of a biologically active 25-mer peptide that
contains the human immunodeficiency virus type 1 Tat basic domain linked
to the core regulatory domain of another lentiviral Tat--i.e., that from
equine infectious anemia virus. Circular dichroism and two-dimensional
proton NMR studies of this hybrid peptide indicate that the Tat basic
domain forms a stable alpha-helix, whereas the adjacent regulatory
sequence is mostly in extended form. These findings suggest that the
tendency to form stable alpha-helices may be a common property of
arginine- and lysine-rich RNA-binding domains.
DE Amino Acid Sequence Binding Sites Circular Dichroism Gene Products,
tat/*CHEMISTRY/*METABOLISM HIV-1/*METABOLISM Models, Structural
Molecular Sequence Data Nuclear Magnetic Resonance/METHODS Peptide
Fragments/*CHEMISTRY/*METABOLISM *Protein Conformation RNA,
Viral/*METABOLISM Software Support, Non-U.S. Gov't Support, U.S.
Gov't, P.H.S. Transcription, Genetic JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).