Abstract
The solution structure of a human immunodeficiency virus type-1 (HIV-1) Rev peptide bound to stem-loop IIB of the Rev response element (RRE) RNA was solved by nuclear magnetic resonance spectroscopy. The Rev peptide has an alpha-helical conformation and binds in the major groove of the RNA near a purine-rich internal loop. Several arginine side chains make base-specific contacts, and an asparagine residue contacts a G.A base pair. The phosphate backbone adjacent to a G.G base pair adopts an unusual structure that allows the peptide to access a widened major groove. The structure formed by the two purine-purine base pairs of the RRE creates a distinctive binding pocket that the peptide can use for specific recognition.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Arginine / chemistry
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Asparagine / chemistry
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Base Composition
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Base Sequence
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DNA-Binding Proteins*
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Fungal Proteins / chemistry
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Gene Products, rev / chemistry*
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Gene Products, rev / metabolism*
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Genes, env*
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HIV-1 / chemistry*
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Hydrogen Bonding
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Sequence Data
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Nucleic Acid Conformation*
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Protein Kinases / chemistry
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Protein Structure, Secondary*
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RNA, Viral / chemistry*
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RNA, Viral / genetics
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RNA, Viral / metabolism
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Saccharomyces cerevisiae Proteins*
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Threonine / chemistry
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rev Gene Products, Human Immunodeficiency Virus
Substances
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DNA-Binding Proteins
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Fungal Proteins
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Gene Products, rev
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RNA, Viral
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Saccharomyces cerevisiae Proteins
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rev Gene Products, Human Immunodeficiency Virus
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Threonine
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Asparagine
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Arginine
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Protein Kinases