Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
THE SOLUTION STRUCTURE OF THE FIRST ZINC-FINGER DOMAIN OF SW15 - A NOVEL STRUCTURAL EXTENSION TO A COMMON FOLD
Autore:
DUTNALL RN; NEUHAUS D; RHODES D;
Indirizzi:
MRC,MOLEC BIOL LAB,HILLS RD CAMBRIDGE CB2 2QH ENGLAND MRC,MOLEC BIOL LAB CAMBRIDGE CB2 2QH ENGLAND
Titolo Testata:
Structure
fascicolo: 5, volume: 4, anno: 1996,
pagine: 599 - 611
SICI:
0969-2126(1996)4:5<599:TSSOTF>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; POTATO CARBOXYPEPTIDASE INHIBITOR; RESOLUTION SOLUTION STRUCTURE; ENHANCER BINDING-PROTEIN; DNA-BINDING; TRANSCRIPTION FACTOR; CRYSTAL-STRUCTURE; 3-DIMENSIONAL STRUCTURE; DISTANCE GEOMETRY; YEAST ADR1;
Keywords:
NMR STRUCTURE; PROTEIN-DNA RECOGNITION; ZINC FINGER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
59
Recensione:
Indirizzi per estratti:
Citazione:
R.N. Dutnall et al., "THE SOLUTION STRUCTURE OF THE FIRST ZINC-FINGER DOMAIN OF SW15 - A NOVEL STRUCTURAL EXTENSION TO A COMMON FOLD", Structure, 4(5), 1996, pp. 599-611

Abstract

Background: The 2Cys-2His (C-2-H-2) zinc finger is a protein domain commonly used for sequence-specific DNA recognition. The zinc fingers of the yeast transcription factors SW15 and ACE2 share strong sequence homology, which extends into a region N-terminal to the first finger, suggesting that the DNA-binding domains of these two proteins include additional structural elements. Results: Structural analysis of the zinc fingers of SW15 reveals that a 15 residue region N-terminal to the finger motifs forms part of the structure of the first finger domain, adding a beta strand and a helix not previously observed in other zincfinger structures. Sequence analysis suggests that other zinc finger proteins may also have this structure. Biochemical studies show that this additional structure increases DNA-binding affinity. Conclusions: The structural analysis presented reveals a novel zinc finger structure in which additional structural elements have been added to the C-2-H-2 zinc finger fold. This additional structure may enhance stability and has implications for DNA recognition by extending the potential DNA-binding surface of a single zinc finger domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 00:55:14