Crystal structure of a prolonged-acting insulin with albumin-binding properties.

@article{Whittingham1997CrystalSO,
  title={Crystal structure of a prolonged-acting insulin with albumin-binding properties.},
  author={Jean L. Whittingham and Svend Havelund and Ib Jonassen},
  journal={Biochemistry},
  year={1997},
  volume={36 10},
  pages={2826-31}
}
The fatty acid acylated insulin, Lys(B29)-tetradecanoyl, des-(B30) human insulin, has been crystallized and the structure determined by X-ray crystallography. The fatty acid substituent on residue B29 Lys binds reversibly to circulating albumin protein in vivo, and by this mechanism the hormone's action is prolonged. Crystals of the fatty acid insulin grow in space group R3, with two dimers in the asymmetric unit, and diffract to 1.8 A spacing. The structure has been solved by molecular… CONTINUE READING

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