Analysis of the conformation and stability of rat TTF-1 homeodomain by circular dichroism.


The conformational stability of TTF-1HD has been determined by CD-monitored thermal denaturation and isothermal urea unfolding studies. The Gibbs free energy of stabilization found are 1.44 and 1.26 kcal.mol-1, respectively. TTF-1HD exhibits a Tm of 42 degrees C and a delta Cp of 80 cal.mol-1.K-1 indicating that TTF-1HD, when free in solution, is a mobile flexible segment folded into loose helices. Such a flexibility would be relevant for the DNA-binding function of this homeodomain. In fact, a small reduction of the alpha-helical content of TTF-1HD significantly modifies its DNA-binding activity. Study holds ProTherm entries: 10388, 10389 Extra Details: homeodomain; circular dichroism; transcription factor; DNA binding;,protein strucure; alpha-helix

Submission Details


Submitter: Connie Wang

Submission Date: April 24, 2018, 8:40 p.m.

Version: 1

Publication Details
Damante G;Tell G;Leonardi A;Fogolari F;Bortolotti N;Di Lauro R;Formisano S,FEBS Lett. (1994) Analysis of the conformation and stability of rat TTF-1 homeodomain by circular dichroism. PMID:7957942
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant PDB Entries

Structure ID Release Date Resolution Structure Title

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Homeobox protein Nkx-2.1 P43699 NKX21_HUMAN
100.0 Homeobox protein Nkx-2.1 P43698 TITF1_CANLF
100.0 Homeobox protein Nkx-2.1 P23441 NKX21_RAT
100.0 Homeobox protein Nkx-2.1 P50220 NKX21_MOUSE
100.0 Homeobox protein Nkx-2.1 Q9H2Z4 NKX24_HUMAN
98.4 Homeobox protein Nkx-2.1 P97273 TITF1_CAVPO
100.0 Homeobox protein Nkx-2.1 Q9EQM3 NKX24_MOUSE