Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Anchoring an extended HTLV-1 Rex peptide within an RNA major groove containing junctional base triples
Autore:
Jiang, F; Gorin, A; Hu, WD; Majumdar, A; Baskerville, S; Xu, WJ; Ellington, A; Patel, DJ;
Indirizzi:
Mem Sloan Kettering Canc Ctr, Cellular Biochem & Biophys Program, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 New York, NY 10021 USA MIT, Whitehead Inst Biomed Res, Cambridge, MA 02142 USA MIT Cambridge MA USA 02142 ehead Inst Biomed Res, Cambridge, MA 02142 USA Univ Texas, Dept Chem, Austin, TX 78712 USA Univ Texas Austin TX USA 78712 niv Texas, Dept Chem, Austin, TX 78712 USA
Titolo Testata:
STRUCTURE WITH FOLDING & DESIGN
fascicolo: 12, volume: 7, anno: 1999,
pagine: 1461 - 1472
SICI:
0969-2126(199912)7:12<1461:AAEHRP>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
T-CELL LEUKEMIA; VIRUS TYPE-I; ARGININE-RICH MOTIF; APTAMER COMPLEX; RESPONSE ELEMENT; MOLECULAR RECOGNITION; NMR STRUCTURE; ALPHA-HELIX; VIRAL-RNA; BINDING;
Keywords:
arginine-guanine sandwich; extended bound basic Rex peptide; flap base; junctional base triples; RNA binding pocket architecture;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Patel, DJ Mem Sloan Kettering Canc Ctr, Cellular Biochem & Biophys Program, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 NY 10021 USA
Citazione:
F. Jiang et al., "Anchoring an extended HTLV-1 Rex peptide within an RNA major groove containing junctional base triples", STRUCT F D, 7(12), 1999, pp. 1461-1472

Abstract

Background: The Rex protein of the human T cell leukemia virus type 1 (HTLV-1) belongs to a family of proteins that use arginine-rich motifs (ARMs) to recognize their RNA targets. Previously, an in vitro selected RNA aptamersequence was identified that mediates mRNA transport in vivo when placed in the primary binding site on stem-loop IID of the Rex response element, Wepresent the solution structure of the HTLV-1 arginine-rich Rex peptide bound to its RNA aptamer target determined by multidimensional heteronuclear NMR spectroscopy,Results: The Rex peptide in a predominantly extended conformation threads through a channel formed by the shallow and widened RNA major groove and a looped out guanine, The RNA aptamer contains three stems separated by a pair of two-base bulges, and adopts an unanticipated fold in which both junctional sites are anchored through base triple formation, Binding specificity is associated with intermolecular hydrogen bonding between guanidinium groups of three non-adjacent arginines and the guanine base edges of three adjacent G.C pairs. Conclusions: The extended S-shaped conformation of the Rex peptide, together with previous demonstrations of a beta-hairpin conformation for the bovine immunodeficiency virus (BIV) Tat peptide and an alpha-helical conformation for the human immunodeficiency virus (HIV) Rev peptide in complex with their respective RNA targets, expands our understanding of the strategies employed by ARMs for adaptive recognition and highlights the importance of RNA tertiary structure in accommodating minimalist elements of protein secondary structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 00:51:14