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Secondary structure of the oct‐3 POU homeodomain as determined by 1 H‐ 15 N NMR spectroscopy
Author(s) -
Morita Eugene H.,
Shirakawa Masahiro,
Hayashi Fumiaki,
Imagawa Masayoshi,
Kyogoku Yoshimasa
Publication year - 1993
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(93)80088-c
Subject(s) - pou domain , heteronuclear molecule , homonuclear molecule , nuclear magnetic resonance spectroscopy , homeobox , helix (gastropod) , chemistry , amide , spectroscopy , crystallography , stereochemistry , nuclear magnetic resonance , physics , biology , molecule , transcription factor , biochemistry , gene , ecology , organic chemistry , snail , quantum mechanics
Most of the 1 H and 15 N 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.