Structural study of rat thyroid transcription factor 1 homeodomain (TTF-1 HD) by nuclear magnetic resonance.

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 Lett

journal_title

FEBS letters

authors

Viglino P,Fogolari F,Formisano S,Bortolotti N,Damante G,Di Lauro R,Esposito G

doi

10.1016/0014-5793(93)80845-l

subject

Has Abstract

pub_date

1993-12-28 00:00:00

pages

397-402

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)80845-L

journal_volume

336

pub_type

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