Abstract
14-3-3 proteins regulate many intracellular processes and their ability to bind in subtly different fashions to their numerous partner proteins provides attractive drug-targeting points for a range of diseases. Schnurri-3 is a suppressor of mouse bone formation and a candidate target for novel osteoporosis therapeutics, and thus it is of interest to determine whether it interacts with 14-3-3. In this work, potential 14-3-3 interaction sites on mammalian Schnurri-3 were identified by an in silico analysis of its protein sequence. Using fluorescence polarization, isothermal titration calorimetry and X-ray crystallography, it is shown that synthetic peptides containing either phosphorylated Thr869 or Ser542 can indeed interact with 14-3-3, with the latter capable of forming an interprotein disulfide bond with 14-3-3σ: a hitherto unreported phenomenon.
| Original language | English |
|---|---|
| Pages (from-to) | 254-261 |
| Number of pages | 8 |
| Journal | Acta Crystallographica Section F: Structural Biology Communications |
| Volume | 77 |
| DOIs | |
| Publication status | Published - 1 Aug 2021 |
Bibliographical note
Funding Information:This work is part of the TASPPI project. The TASPPI project is supported by the Initial Training Network (ITN) initiative, funded by the H2020 Marie Curie Actions of the European Commission under Grant Agreement 675179.
Funding
This work is part of the TASPPI project. The TASPPI project is supported by the Initial Training Network (ITN) initiative, funded by the H2020 Marie Curie Actions of the European Commission under Grant Agreement 675179.
| Funders | Funder number |
|---|---|
| Marie Skłodowska‐Curie | |
| European Union's Horizon 2020 - Research and Innovation Framework Programme | |
| European Commission | 675179 |
Keywords
- 14-3-3 modes
- bone regulator protein
- disulfide bonds
- fluorescence polarization
- phosphorylation
- Schnurri-3
- X-ray protein crystallography