Secondary structure of the oct-3 POU homeodomain as determined by 1H-15N NMR spectroscopy.
Most of the 1H and 15N magnetic resonances of the 66 amino acid long POU homeodomain of mouse Oct-3 have been assigned by the combined use of the two-dimensional homonuclear, and two- and three-dimensional heteronuclear NMR methods. The sequential NOE connectivities and amide proton exchange measurements indicate the presence of three helical regions within the domain. The positions of the three helices correspond well to those of other homeodomains, the three-dimensional structures of which have already been determined. The present NMR study provides the first experimental evidence for the existence of a helix-turn-helix motif in the oct-3 POU homeodomain.
Morita
E H
EH
Institute for Protein Research, Osaka University, Japan.
Shirakawa
M
M
Hayashi
F
F
Imagawa
M
M
Kyogoku
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D005801:Genes, Homeobox; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D051379:Mice; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D050814:Octamer Transcription Factor-3; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D004268:DNA-Binding Proteins; D009587:Nitrogen Isotopes; D050814:Octamer Transcription Factor-3; C494174:Pou5f1 protein, mouse; D011994:Recombinant Proteins; D014157:Transcription Factors; D006859:Hydrogen