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• W3040729519 endingPage "140485" @default.
• W3040729519 startingPage "140485" @default.
• W3040729519 abstract "The proper orchestration of transforming growth factor beta (TGFβ) mediated signal transduction depends upon a delicate set of interactions between specific ligands and their receptors. Here we present an in-depth profiling of the binding mechanism of TGFβ3 ligand with its type II and type I receptors (TβRII and TβRI) using isothermal titration calorimetry (ITC). Studies were carried out in acidic pH as it has great physiological relevance for TGFβ3 activity. Our findings reveal an unusual positive enthalpy (∆H) compensated by a large favourable entropy (∆S) during TGFβ3-TβRII interaction. In addition to the hydrophobic effect, we propose that a distinct conformational switch from closed to open form as experienced by TGFβ3 on binding to TβRII is contributing significantly to the increase in overall entropy of the system. Binding studies of TGFβ3 and TβRII were carried out at different pH values and salt concentrations to gain further insight into the thermodynamics of the interaction. Furthermore, the importance of hydrophobic interactions on the binding affinity of TβRII with TGFβ3 was confirmed by two TβRII variants (interfacial). Finally, a distinct shift from entropy to enthalpy dominated interaction was observed upon recruitment of TβRI to the binary complex forming the ternary complex." @default.
• W3040729519 created "2020-07-16" @default.
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• W3040729519 date "2020-11-01" @default.
• W3040729519 modified "2023-10-17" @default.
• W3040729519 title "Interaction of TGFβ3 ligand with its receptors type II (TβRII) and type I (TβRI): A unique mechanism of protein-protein association" @default.
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• W3040729519 doi "https://doi.org/10.1016/j.bbapap.2020.140485" @default.
• W3040729519 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32652126" @default.
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