Design of a cyclic peptide that targets a viral RNA.
The Tat protein controls transcription in lentiviruses such as HIV. A cyclic peptide analog of the RNA binding domain of the bovine immunodeficiency virus (BIV) Tat protein is shown to bind specifically to its target RNA stem loop. NMR data indicate a similar mode of binding of linear and cyclic peptides.
Runyon
Steven T
ST
Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, USA.
Puglisi
Joseph D
JD
D000818:Animals; D002417:Cattle; D015195:Drug Design; D015696:Gene Products, tat / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D016087:Immunodeficiency Virus, Bovine / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D011487:Protein Conformation; D012367:RNA, Viral / Q000187:drug effects / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D013379:Substrate Specificity
D015696:Gene Products, tat; D010446:Peptide Fragments; D010456:Peptides, Cyclic; D012367:RNA, Viral; D016601:RNA-Binding Proteins