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Titolo:
HIGH-RESOLUTION STRUCTURES OF VARIANT ZIF268-DNA COMPLEXES - IMPLICATIONS FOR UNDERSTANDING ZINC-FINGER DNA RECOGNITION
Autore:
ELRODERICKSON M; BENSON TE; PABO CO;
Indirizzi:
MIT,DEPT BIOL,77 MASSACHUSETTS AVE CAMBRIDGE MA 02139 MIT,DEPT BIOL CAMBRIDGE MA 02139 MIT,HOWARD HUGHES MED INST CAMBRIDGE MA 02139
Titolo Testata:
Structure
fascicolo: 4, volume: 6, anno: 1998,
pagine: 451 - 464
SICI:
0969-2126(1998)6:4<451:HSOVZC>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; SELECTION; SITE; ERRORS; PHAGE; RULES; MAPS;
Keywords:
PROTEIN-DNA RECOGNITION; X-RAY CRYSTALLOGRAPHY; ZIF268; ZINC FINGER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
M. Elroderickson et al., "HIGH-RESOLUTION STRUCTURES OF VARIANT ZIF268-DNA COMPLEXES - IMPLICATIONS FOR UNDERSTANDING ZINC-FINGER DNA RECOGNITION", Structure, 6(4), 1998, pp. 451-464

Abstract

Background: Zinc fingers of the Cys(2)-His(2) Glass comprise one of the largest families of eukaryotic DNA-binding motifs and recognize a diverse set of DNA sequences, These proteins have a relatively simple modular structure and key base contacts are typically made by a few residues from each finger. These features make the zinc finger motif an attractive system for designing novel DNA-binding proteins and for exploring fundamental principles of protein-DNA recognition, Results: Herewe report the X-ray crystal structures of zinc finger-DNA complexes involving three variants of Zif268, with multiple changes in the recognition helix of finger one. We describe the structure of each of these three-finger peptides bound to its corresponding target site. To help elucidate the differential basis for site-specific recognition, the structures of four other complexes containing various combinations of these peptides with alternative binding sites have also been determined,Conclusions: The protein-DNA contacts observed in these complexes reveal the basis for the specificity demonstrated by these Zif268 variants. Many, but not all, of the contacts can be rationalized in terms of a recognition code, but the predictive value of such a code is limited, The structures illustrate how modest changes in the docking arrangement accommodate the new sidechain-base and sidechain-phosphate interactions. Such adaptations help explain the versatility of naturally occurring zinc finger proteins and their utility in design.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 07:33:41