Congrats to Dr. Chao Feng for new publication
Congrats to Dr. Chao Feng for new publication on Protein Science:
Feng C, Roy A, Post CB (2018) Entropic allostery dominates the phosphorylation-dependent regulation of Syk tyrosine kinase release from immunoreceptor tyrosine-based activation motifs: Entropic Allostery Dominates Syk Release. Protein Science 27:1780–1796. [doi] [pdf]
It is highlighted in “In This Issue” as follows: https://onlinelibrary.wiley.com/doi/full/10.1002/pro.3538
Tyrosine phosphorylation is key to the regulation of numerous cellular processes. Phosphorylation is known to control protein function through direct interaction of tyrosine that favors either the phosphorylated or unphosphorylated form of the protein. In this paper, we report a previously unknown mechanism for controlling protein protein association by phosphorylation. NMR and thermodynamic investigations of Syk tyrosine kinase binding membrane immune receptors find that phosphorylation actually has negligible effect on the interactions stabilizing the complex. Instead, phosphorylation increases the randomness of unbound Syk so that formation of the complex imposes a higher entropic penalty, without perturbing bound interactions. This consequence of phosphorylation is therefore fully entropically based.