Abstract:
:Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) interacts with and inhibits the tumor suppressor function of prohibitin-2 (PHB2), and recent in vivo studies have demonstrated that the BIG3-PHB2 interaction is a promising target for breast cancer therapy. However, little biophysical characterization on BIG3 and its interaction with PHB2 has been reported. Here we compared the calculated 8-class secondary structure of the N-terminal domains of BIG family proteins and identified a loop region unique to BIG3. Our biophysical characterization demonstrated that this loop region significantly affects the colloidal and thermodynamic stability of BIG3 and the thermodynamic and kinetic profile of its interaction with PHB2. These results establish a model for the BIG3-PHB2 interaction and an entry for drug discovery for breast cancer.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Chigira T,Nagatoishi S,Takeda H,Yoshimaru T,Katagiri T,Tsumoto Kdoi
10.1016/j.bbrc.2019.08.028subject
Has Abstractpub_date
2019-10-08 00:00:00pages
183-189issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(19)31539-6journal_volume
518pub_type
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