How Tat targets TAR: structure of the BIV peptide-RNA complex.
Two new NMR structures describing the complex formed by a peptide from the BIV Tat protein with the TAR RNA provide a significant advance in our understanding of the ways in which peptides interact with specific sites in the major groove of their RNA targets.
Greenbaum
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Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D015696:Gene Products, tat / Q000737:chemistry* / Q000378:metabolism; D015497:HIV-1 / Q000737:chemistry; D016087:Immunodeficiency Virus, Bovine / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D054322:tat Gene Products, Human Immunodeficiency Virus; D000099253:Trans-Activation Responsive RNA-Binding Protein
D015696:Gene Products, tat; D012313:RNA; D016601:RNA-Binding Proteins; D054322:tat Gene Products, Human Immunodeficiency Virus; D000099253:Trans-Activation Responsive RNA-Binding Protein