The structure of a mutant insulin uncouples receptor binding from protein allostery. An electrostatic block to the TR transition.

@article{Wan2008TheSO,
  title={The structure of a mutant insulin uncouples receptor binding from protein allostery. An electrostatic block to the TR transition.},
  author={Zhu-li Wan and Kun Huang and Shi-quan Hu and Jonathan Whittaker and Michael A Weiss},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 30},
  pages={
          21198-210
        }
}
The zinc insulin hexamer undergoes allosteric reorganization among three conformational states, designated T(6), T(3)R(3)(f), and R(6). Although the free monomer in solution (the active species) resembles the classical T-state, an R-like conformational change is proposed to occur upon receptor binding. Here, we distinguish between the conformational requirements of receptor binding and the crystallographic TR transition by design of an active variant refractory to such reorganization. Our… CONTINUE READING
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