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

Paolo Viglino, Federico Fogolari, Silvestro Formisano, Nadia Bortolotti, Giuseppe Damante, Roberto Di Lauro, Gennaro Esposito

Research output: Contribution to journalArticlepeer-review

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-tum-helix motif commonly occurring in many classes of DNA-binding proteins.

Original languageEnglish (US)
Pages (from-to)397-402
Number of pages6
JournalFEBS Letters
Volume336
Issue number3
DOIs
StatePublished - Dec 28 1993

Keywords

  • Homeodomain
  • Protein NMR
  • Thyroid transcription factor 1 (TTF-1)

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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