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Titolo:
Beyond the "recognition code": Structures of two Cys(2)His(2) zinc finger/TATA box complexes
Autore:
Wolfe, SA; Grant, RA; Elrod-Erickson, M; Pabo, CO;
Indirizzi:
MIT, Howard Hughes Med Inst, Dept Biol, Cambridge, MA 02139 USA MIT Cambridge MA USA 02139 s Med Inst, Dept Biol, Cambridge, MA 02139 USA
Titolo Testata:
STRUCTURE
fascicolo: 8, volume: 9, anno: 2001,
pagine: 717 - 723
SICI:
0969-2126(200108)9:8<717:BT"CSO>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; DNA RECOGNITION; PHAGE DISPLAY; PROTEIN; SEQUENCES; GROOVE; SITE;
Keywords:
protein-DNA recognition; TATA box; X-ray crystallography; zinc finger; recognition code;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Pabo, CO MIT, Howard Hughes Med Inst, Dept Biol, 77 Massachusetts Ave, Cambridge, MA 02139 USA MIT 77 Massachusetts Ave Cambridge MA USA 02139 dge, MA 02139 USA
Citazione:
S.A. Wolfe et al., "Beyond the "recognition code": Structures of two Cys(2)His(2) zinc finger/TATA box complexes", STRUCTURE, 9(8), 2001, pp. 717-723

Abstract

Background: Several methods have been developed for creating Cys(2)His(2) zinc finger proteins that recognize novel DNA sequences, and these proteinsmay have important applications in biological research and gene therapy. In spite of this progress with design/selection methodology, fundamental questions remain about the principles that govern DNA recognition. One hypothesis suggests that recognition can be described by a simple set of rules-essentially a "recognition code"-but careful assessment of this proposal has been difficult because there have been few structural studies of selected zinc finger proteins. Results: We report the high-resolution cocrystal structures of two zinc finger proteins that had been selected (as variants of Zif268) to recognize aeukaryotic TATA box sequence. The overall docking arrangement of the fingers within the major groove of the DNA is similar to that observed in the Zif268 complex. Nevertheless, comparison of Zif268 and the selected variants reveal significant differences in the pattern of side chain-base interactions. The new structures also reveal side chain-side chain interactions (bothwithin and between fingers) that are important in stabilizing the protein-DNA interface and appear to play substantial roles in recognition. Conclusions: These new structures highlight the surprising complexity of zinc finger-DNA interactions. The diversity of interactions observed at the protein-DNA interface, which is especially striking for proteins that were all derived from Zif268, challenges fundamental concepts about zinc finger-DNA recognition and underscores the difficulty in developing any meaningfulrecognition code.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 23:26:16