Binding of a cyclic BIV beta-Tat peptide with its TAR RNA construct.
The ability of RNA structures to adopt diverse yet complex tertiary structures has resulted in numerous fascinating RNA-protein recognition events. It was recently reported that a close relative of the HIV Rev peptide, namely a 17 residue Tat peptide from bovine immuno-deficiency virus (BIV), is able to bind to the 28 nucleotide BIV TAR RNA construct. Here we report that by simply converting the 17 residue beta-ribbon peptide structure to a 19 residue cyclopeptide, the binding affinity (Kd) of the resulting cyclopeptide to the TAR RNA target, observed by fluorescence binding study, was enhanced approximately 5-fold.
Tok
J B
JB
Department of Chemistry, Indiana University-Purdue University, Fort Wayne, 46805, USA. tokj@ipfw.edu
Des Jean
R C
RC
Fenker
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D019793:Fluorescein; D005453:Fluorescence; D015696:Gene Products, tat / Q000737:chemistry / Q000378:metabolism*; D016325:HIV Long Terminal Repeat / Q000235:genetics*; D016087:Immunodeficiency Virus, Bovine / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D010456:Peptides, Cyclic / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics
D015696:Gene Products, tat; D010446:Peptide Fragments; D010456:Peptides, Cyclic; D012367:RNA, Viral; D016601:RNA-Binding Proteins; D019793:Fluorescein