Structural and mutational analysis of affinity-inert contact residues at the growth hormone-receptor interface.

@article{Pearce1996StructuralAM,
  title={Structural and mutational analysis of affinity-inert contact residues at the growth hormone-receptor interface.},
  author={Kenneth H. Pearce and Mark H. Ultsch and Robert F. Kelley and Abraham M de Vos and James A. Wells},
  journal={Biochemistry},
  year={1996},
  volume={35 32},
  pages={10300-7}
}
Mutational studies have shown that over two-thirds of the contact side chains at the human growth hormone (hGH)-receptor interface have little or no impact on binding affinity when converted to alanine [Cunningham, B. C., & Wells, J. A. (1993) J. Mol. Biol. 234, 554-563; Clackson, T., & Wells, J. A. (1995) Science 267. 383-386]. Herein, three of the most buried, yet functionally inert, residues on hGH (F25, Y42, and Q46) have been simultaneously mutated to alanine. Binding kinetics of the… CONTINUE READING

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