A conserved histidine in insulin is required for the foldability of human proinsulin: structure and function of an ALAB5 analog.

@article{Hua2006ACH,
  title={A conserved histidine in insulin is required for the foldability of human proinsulin: structure and function of an ALAB5 analog.},
  author={Qing-xin Hua and Ming Liu and Shi-quan Hu and Wenhua Jia and Peter Arvan and Michael A Weiss},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 34},
  pages={24889-99}
}
The insulins of eutherian mammals contain histidines at positions B5 and B10. The role of His(B10) is well defined: although not required in the mature hormone for receptor binding, in the islet beta cell this side chain functions in targeting proinsulin to glucose-regulated secretory granules and provides axial zincbinding sites in storage hexamers. In contrast, the role of His(B5) is less well understood. Here, we demonstrate that its substitution with Ala markedly impairs insulin chain… CONTINUE READING

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