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Secondary structure and folding topology of the DNA binding domain of interferon regulatory factor 2, as revealed by NMR spectroscopy
Author(s) -
Uegaki Koichi,
Shirakawa Masahiro,
Harada Hisashi,
Taniguchi Tadatsugu,
Kyogoku Yoshimasa
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00040-g
Subject(s) - folding (dsp implementation) , topology (electrical circuits) , nuclear magnetic resonance spectroscopy , chemistry , dna binding domain , dna , domain (mathematical analysis) , biophysics , protein folding , spectroscopy , biochemistry , biology , stereochemistry , gene , physics , transcription factor , mathematics , combinatorics , quantum mechanics , mathematical analysis , electrical engineering , engineering
The secondary structure elements of the DNA‐binding domain of mouse interferon regulatory factor 2 [IRF‐2(113)] were determined by heteronuclear multidimensional NMR spectroscopy. The sequential NOE connectivities, amide proton exchange rates, and 3 J HNα coupling constants indicated the presence of three α‐helical regions and four short β‐strands connected through 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 proteins, although there is no sequence homology among them.