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

doi:10.1016/0014-5793(93)80845-L

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

Chemistry

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	397-402
Number of pages	6
Journal	FEBS Letters
Volume	336
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(93)80845-L
State	Published - 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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10.1016/0014-5793(93)80845-L

Cite this

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AU - Viglino, Paolo

AU - Fogolari, Federico

AU - Formisano, Silvestro

AU - Bortolotti, Nadia

AU - Damante, Giuseppe

AU - Di Lauro, Roberto

AU - Esposito, Gennaro

PY - 1993/12/28

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AB - 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.

KW - Homeodomain

KW - Protein NMR

KW - Thyroid transcription factor 1 (TTF-1)

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

Abstract

Keywords

ASJC Scopus subject areas

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