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Titolo:
Crystal structure of MEF2A core bound to DNA at 1.5 angstrom resolution
Autore:
Santelli, E; Richmond, TJ;
Indirizzi:
ETH Zurich, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland ETH Zurich Zurich Switzerland CH-8093 ophys, CH-8093 Zurich, Switzerland
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 2, volume: 297, anno: 2000,
pagine: 437 - 449
SICI:
0022-2836(20000324)297:2<437:CSOMCB>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTOR MEF2C; HEAVY-CHAIN GENE; BINDING SPECIFICITY; ENHANCER FACTOR-2; MYOGENIC LINEAGE; NONMUSCLE CELLS; MUSCLE; ACTIVATION; EXPRESSION; PROTEINS;
Keywords:
transcription factor; muscle development; protein-DNA recognition; MADS-box; X-ray crystallography;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Richmond, TJ ETH Zurich, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland ETH Zurich Zurich Switzerland CH-8093 3 Zurich, Switzerland
Citazione:
E. Santelli e T.J. Richmond, "Crystal structure of MEF2A core bound to DNA at 1.5 angstrom resolution", J MOL BIOL, 297(2), 2000, pp. 437-449

Abstract

Members of the myocyte enhancer factor-2 (MEF2) family of transcription factors bind to and activate transcription through A + T-rich DNA sequences found primarily, but not exclusively, in the promoters of muscle-specific genes. Their importance has been established for myogenic development and in activation of the immediate-early gene, c-jun, and recently further functional roles in the immune system have emerged. The MEF2 factors belong to theMADS-box superfamily, sharing homology in a 58 amino acid domain that mediates DNA binding and dimerization. The structures of two MADS-box proteins,SRF and MCM1, bound to their cognate DNA have been previously reported andshown to share extensive similarity in their mode of DNA binding. We have solved the structure of MEF2A 2-78 bound to its DNA consensus sequence at 1.5 Angstrom resolution. It reveals how the absence of amino acids N-terminal to the MADS-box contributes to the DNA binding properties of MEF2 proteins and shows that the MEF domain C-terminal to the MADS-box adopts a conformation considerably different from the same region in SRF and MCM1. (C) 2000Academic Press.

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Documento generato il 28/09/20 alle ore 15:42:27