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Titolo:
Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0
Autore:
Nagata, T; Kurihara, Y; Matsuda, G; Saeki, J; Kohno, T; Yanagida, Y; Ishikawa, F; Uesugi, S; Katahira, M;
Indirizzi:
Yokohama,Natl Univ, Fac Engn, Dept Chem & Biotechnol, Hodogaya Ku, Yokohama Yokohama Natl Univ Yokohama Kanagawa Japan 2408501 Hodogaya Ku, Yokohama Mitsubishi Kasei Inst Life Sci, Tokyo 1948511, Japan Mitsubishi Kasei InstLife Sci Tokyo Japan 1948511 Tokyo 1948511, Japan Tokyo Inst Technol, Dept Bioengn, Midori Ku, Yokohama, Kanagawa 226, JapanTokyo Inst Technol Yokohama Kanagawa Japan 226 ohama, Kanagawa 226, Japan Tokyo Inst Technol, Dept Life Sci, Midori Ku, Yokohama, Kanagawa 226, Japan Tokyo Inst Technol Yokohama Kanagawa Japan 226 ohama, Kanagawa 226, Japan
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 2, volume: 287, anno: 1999,
pagine: 221 - 237
SICI:
0022-2836(19990326)287:2<221:SAIWRO>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; HUMAN U1A PROTEIN; CRYSTAL-STRUCTURE; NMR-SPECTROSCOPY; SEX-LETHAL; DISTANCE GEOMETRY; H-1-NMR SPECTRA; MESSENGER-RNA; C-PROTEINS; ANGSTROM RESOLUTION;
Keywords:
RNA-binding protein; hnRNP; RNA-protein interaction; quadruplex; NMR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Uesugi, S Yokohamaiwadai,niv, Fac Engn, Dept Chem & Biotechnol, Hodogaya Ku, 79-5 Tok Yokohama Natl Univ 79-5 Tokiwadai Yokohama Kanagawa Japan 2408501
Citazione:
T. Nagata et al., "Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0", J MOL BIOL, 287(2), 1999, pp. 221-237

Abstract

Heterogeneous nuclear ribonucleoprotein (hnRNP) DO has two ribonucleoprotein (RNP)-type RNA-binding domains (RBDs), each of which can bind solely to the UUAG sequence specifically. The structure of the N-terminal RED (RBD1) determined by NMR is presented here. It folds into a compact alpha beta structure comprising a four-stranded antiparallel beta-sheet packed against two alpha-helices, which is characteristic of the RNP-type RBDs. Special structural features of RBD1 include N-capping boxes for both alpha-helices, a beta-bulge in the second beta-strand, and an additional short antiparallel beta-sheet coupled with a beta-turn-like structure in a loop. Two hydrogen bonds which restrict the positions of loops were identified. Backbone resonance assignments for RBD1 complexed with r(UUAGGG) revealed that the overallfolding is maintained in the complex. The candidate residues involved in the interactions with RNA were identified by chemical shift perturbation analysis. They are located in the central and peripheral regions of the RNA-binding surface composed of the four-stranded beta-sheet, loops, and the C-terminal region. It is suggested that non-specific interactions with RNA are performed by the residues in the central region of the RNA-binding surface,while specific interactions are performed by those in the peripheral regions. It was also found that RBD1 has the ability to inhibit the formation ofthe quadruplex structure. (C) 1999 Academic Press.

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Documento generato il 05/07/20 alle ore 07:38:26