Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex

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Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex.

BACKGROUND In lentiviruses such as human immunodeficiency virus (HIV) and bovine immunodeficiency virus (BIV), the Tat (trans-activating) protein enhances transcription of the viral RNA by complexing to the 5'-end of the transcribed mRNA, at a region known as TAR (the trans-activation response element). Identification of the determinants that account for specific molecular recognition requires ...

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Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex.

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...

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Molecular dynamics and binding specificity analysis of the bovine immunodeficiency virus BIV Tat-TAR complex.

We have performed molecular dynamics (MD) simulations, with particle-mesh Ewald, explicit waters, and counterions, and binding specificity analyses using combined molecular mechanics and continuum solvent (MM-PBSA) on the bovine immunodeficiency virus (BIV) Tat peptide-TAR RNA complex. The solution structure for the complex was solved independently by Patel and co-workers and Puglisi and co-wor...

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An RNA-binding peptide from bovine immunodeficiency virus Tat protein recognizes an unusual RNA structure.

The human immunodeficiency virus (HIV) Tat protein binds specifically to an RNA hairpin, TAR, located at the 5' end of its mRNA. Tat uses a single arginine residue within a short region of basic amino acids to recognize a bulge region in TAR. Here we show that a 17 amino acid arginine-rich peptide from the bovine immunodeficiency virus (BIV) Tat protein also binds to an RNA hairpin at the 5' en...

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ژورنال

عنوان ژورنال: Chemistry & Biology

سال: 1995

ISSN: 1074-5521

DOI: 10.1016/1074-5521(95)90089-6