Unique Structure of the DNA Binding Domain of Interferon Regulatory Factor 2 Determined by NMR Spectroscopy.

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概要

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• The secondary structure elements and the folding topology of the DNA-binding domain of mouse interferon regulatory factor 2 [IRF-2(113)] were determined by heteronuclear multidimensional NMR spectroscopy. The sequential NOE (nuclear Overhauser effect) connectivities indicated the presence of three α-helical regions and four short β-strands connected by relatively long loops. The long range NOEs indicated the four strands form an antiparallel β-sheet and the three α-helices form a bundle on the sheet. The arrangement of the secondary structure elements and the overall folding topology resemble those of the DNA binding domains of bacterial activator CAP, heat shock transcription factors and fork-head family transcription factors, although there is no sequence homology among them.

• 日本学士院の論文

著者

• SHIRAKAWA Masahiro

  Institute for Protein Research, Osaka University

関連論文

• Unique Structure of the DNA Binding Domain of Interferon Regulatory Factor 2 Determined by NMR Spectroscopy.

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