Abstract:
:The 500 MHz 1H 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-turn-helix motif commonly occurring in many classes of DNA-binding proteins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Viglino P,Fogolari F,Formisano S,Bortolotti N,Damante G,Di Lauro R,Esposito Gdoi
10.1016/0014-5793(93)80845-lsubject
Has Abstractpub_date
1993-12-28 00:00:00pages
397-402issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(93)80845-Ljournal_volume
336pub_type
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