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Titolo:
CRYSTAL-STRUCTURE OF A BZIP DNA COMPLEX AT 2.2 ANGSTROM - DETERMINANTS OF DNA SPECIFIC RECOGNITION/
Autore:
KELLER W; KONIG P; RICHMOND TJ;
Indirizzi:
ETH ZURICH,INST MOLEK BIOL & BIOPHYS,HONGGERBERG CH-8093 ZURICH SWITZERLAND ETH ZURICH,INST MOLEK BIOL & BIOPHYS CH-8093 ZURICH SWITZERLAND
Titolo Testata:
Journal of Molecular Biology
fascicolo: 4, volume: 254, anno: 1995,
pagine: 657 - 667
SICI:
0022-2836(1995)254:4<657:COABDC>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
X-RAY STRUCTURE; LEUCINE ZIPPER; ACTIVATOR PROTEIN; BINDING PROTEINS; GCN4 PROTEIN; YEAST; REPRESSOR; REFINEMENT; RESOLUTION; SEQUENCES;
Keywords:
PROTEIN-DNA RECOGNITION; BZIP/GCN4; TRANSCRIPTION FACTOR; X-RAY CRYSTALLOGRAPHY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
W. Keller et al., "CRYSTAL-STRUCTURE OF A BZIP DNA COMPLEX AT 2.2 ANGSTROM - DETERMINANTS OF DNA SPECIFIC RECOGNITION/", Journal of Molecular Biology, 254(4), 1995, pp. 657-667

Abstract

The X-ray structure of the GCN4-bZIP protein bound to DNA containing the ATF/CREB recognition sequence has been refined at 2.2 Angstrom. The water-mediated interactions between the basic domain and DNA are revealed, and combined with a more accurate description of the direct contacts, further clarify how binding specificity is achieved. Water molecules extend the interactions of both invariant basic domain residues,asparagine 235 and arginine 243, beyond their direct base contacts. The slight bending of the basic domain alpha-helix around the DNA facilitates the linking of arginine 241, 243 and 245 to main-chain carbonyloxygen atoms via water molecules, apparently stabilizing interactionswith the DNA. (C) 1995 Academic Press Limited

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 13:56:51