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Structural study of rat thyroid transcription factor 1 homeodomain (TTF‐1 HD) by nuclear magnetic resonance
Author(s) -
Viglino Paolo,
Fogolari Federico,
Formisano Silvestro,
Bortolotti Nadia,
Damante Giuseppe,
Di Lauro Roberto,
Esposito Gennaro
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)80845-l
Subject(s) - homeobox , transcription factor , helix (gastropod) , chemistry , peptide , thyroid transcription factor 1 , basic helix loop helix , nuclear magnetic resonance , crystallography , biology , gene , dna binding protein , biochemistry , physics , ecology , snail
The 500 MHz 1 H NMR spectrum of a 68‐residue peptide, encompassing the rat thyroid transcription factor 1 homeodomain (TTF‐1 HD), was fully assigned using standard 2D NMR methodology. The secondary structure elements and their spatial organization were determined and led to a structure very similar to that previously described for other homeodomains and expected also for TTF‐1 HD from homology modeling predictions. The three‐dimensional arrangement of the three helix fragments of TTF‐1 HD preserves the helix‐tum‐helix motif commonly occurring in many classes of DNA‐binding proteins.