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 UniProtKB Entries

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