Transforming Growth Factor Receptor Type II (ec-TßR II) behaves as a halophile.

International journal of biological macromolecules

PubMedID: 25316422

Saini K, Khan MA, Chakrapani S, Deep S. Transforming Growth Factor Receptor Type II (ec-TßR II) behaves as a halophile. Int J Biol Macromol. 2014;.
The members of transforming growth factor ß family (TGF-ß) are multifunctional proteins but their main role is to control cell proliferation and differentiation. Polypeptides of TGF-ß family function by binding to two related, functionally distinct transmembrane receptor kinases, first to the type II (TßR II) followed by type I receptor (TßR I). The paper describes, in details, the stability of wt-ec-TßR II under different conditions. The stability of wt-ec-TßR II was observed at different pH and salt concentration using fluorescence spectroscopy. Stability of ec-TßR II decreases with decrease in pH. Interestingly, the addition of salt increases the stability of the TßRII at pH 5.0 as observed for halophiles. Computational analysis using DELPHI suggests that this is probably due to the decrease in repulsion between negatively charged residues at surface on the addition of salt. This is further confirmed by the change in the stability of receptor on mutation of some of the residues (D32A) at surface.