Aromatic anchor at an invariant hormone-receptor interface: function of insulin residue B24 with application to protein design.

@article{Pandyarajan2014AromaticAA,
  title={Aromatic anchor at an invariant hormone-receptor interface: function of insulin residue B24 with application to protein design.},
  author={Vijay Pandyarajan and Brian J Smith and Nelson F B Phillips and Linda J. Whittaker and Gabriella P Cox and Nalinda P. Wickramasinghe and John G. T. Menting and Zhu-li Wan and Jonathan Whittaker and Faramarz Ismail-Beigi and Michael C Lawrence and Michael A Weiss},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 50},
  pages={
          34709-27
        }
}
Crystallographic studies of insulin bound to fragments of the insulin receptor have recently defined the topography of the primary hormone-receptor interface. Here, we have investigated the role of Phe(B24), an invariant aromatic anchor at this interface and site of a human mutation causing diabetes mellitus. An extensive set of B24 substitutions has been constructed and tested for effects on receptor binding. Although aromaticity has long been considered a key requirement at this position, Met… CONTINUE READING
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