Solution structure of the MEF2A–DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors
AUTOR(ES)
Huang, Kai
FONTE
Oxford University Press
RESUMO
The solution structure of the 33 kDa complex between the dimeric DNA-binding core domain of the transcription factor MEF2A (residues 1–85) and a 20mer DNA oligonucleotide comprising the consensus sequence CTA(A/T)4TAG has been solved by NMR. The protein comprises two domains: a MADS-box (residues 1–58) and a MEF2S domain (residues 59–73). Recognition and specificity are achieved by interactions between the MADS-box and both the major and minor grooves of the DNA. A number of critical differences in protein–DNA contacts observed in the MEF2A–DNA complex and the DNA complexes of the related MADS-box transcription factors SRF and MCM1 provide a molecular explanation for modulation of sequence specificity and extent of DNA bending (∼15 versus ∼70°). The structure of the MEF2S domain is entirely different from that of the equivalent SAM domain in SRF and MCM1, accounting for the absence of cross-reactivity with other proteins that interact with these transcription factors.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=212754Documentos Relacionados
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