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Titolo:
3-DIMENSIONAL STRUCTURE OF THE STAT3-BETA HOMODIMER BOUND TO DNA
Autore:
BECKER S; GRONER B; MULLER CW;
Indirizzi:
EUROPEAN MOL BIOL LAB,GRENOBLE OUTSTN,ILL BP 156 F-38042 GRENOBLE 9 FRANCE EUROPEAN MOL BIOL LAB,GRENOBLE OUTSTN F-38042 GRENOBLE 9 FRANCE INST EXPT CANC RES,TUMOR BIOL CTR D-79106 FREIBURG GERMANY
Titolo Testata:
Nature
fascicolo: 6689, volume: 394, anno: 1998,
pagine: 145 - 151
SICI:
0028-0836(1998)394:6689<145:3SOTSH>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
B P50 HOMODIMER; ELECTRON-DENSITY MAPS; TRANSCRIPTIONAL ACTIVITY; SIGNAL TRANSDUCERS; TROPONIN-C; BINDING; STAT; DOMAIN; RECOGNITION; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
S. Becker et al., "3-DIMENSIONAL STRUCTURE OF THE STAT3-BETA HOMODIMER BOUND TO DNA", Nature, 394(6689), 1998, pp. 145-151

Abstract

STAT proteins are a family of eukaryotic transcription factors that mediate the response to a large number of cytokines and growth factors. Upon activation by cell-surface receptors or their associated kinases, STAT proteins dimerize, translocate to the nucleus and bind to specific promoter sequences on their target genes. Here we report the firstcrystal structure of a STAT protein bound to its DNA recognition siteat 2.25 Angstrom resolution. The structure provides insight into the various steps by which STAT proteins deliver a response signal directly from the cell membrane to their target genes in the nucleus.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 22:16:55