1FTT

THYROID TRANSCRIPTION FACTOR 1 HOMEODOMAIN (RATTUS NORVEGICUS)

1FTT の概要

• エントリーDOI: 10.2210/pdb1ftt/pdb
• 分子名称: THYROID TRANSCRIPTION FACTOR 1 HOMEODOMAIN (1 entity in total)
• 機能のキーワード: dna binding protein, homeodomain, transcription factor
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Nucleus: P23441
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8463.92

構造登録者

Fogolari, F.,Esposito, G.,Damante, G.,Formisano, S.,Di Lauro, R.,Viglino, P. (登録日: 1995-10-03, 公開日: 1996-01-29, 最終更新日: 2024-05-22)

主引用文献

Esposito, G.,Fogolari, F.,Damante, G.,Formisano, S.,Tell, G.,Leonardi, A.,Di Lauro, R.,Viglino, P.
Analysis of the solution structure of the homeodomain of rat thyroid transcription factor 1 by 1H-NMR spectroscopy and restrained molecular mechanics.
Eur.J.Biochem., 241:101-113, 1996

PubMed Abstract: The solution structure of the rat thyroid transcription factor 1 (TTF-1) homeodomain has been elucidated by 1H-NMR and restrained modeling. The TTF-1 homeodomain folds in the same manner as classical homeodomains, with three helices, a loose loop between the first two helices, and a tight turn between helix II and helix III. The typical assembly of the hydrophobic core is maintained and N-capping motifs are identified in helix I and helix III. The N-terminal stretch of helix II exhibits some mobility, similar to the preceding loop region, which may be related to its anomalous capping. The N-terminal decapeptide and the C-terminal octapeptide of the molecule (68 residues long) are disordered. All the previous characteristics are shared by all known isolated homeodomain structures. An important difference among these structures occurs at the C-terminal extension of helix III, which is either disordered or helically folded. In the TTF-1 homeodomain, the C-terminal extension of helix III (residues 51-59) appears structured, albeit not as rigidly as the preceding portion. Analysis of the NOEs and hydrogendeuterium exchange of backbone amides provides evidence for discontinuity between the two moieties of helix III, which is introduced by a tightening or a kink of residues 51-53.

PubMed: 8898894
DOI: 10.1111/j.1432-1033.1996.0101t.x

実験手法

SOLUTION NMR