Crystal structure of human chorionic gonadotropin

@article{Lapthorn1994CrystalSO,
  title={Crystal structure of human chorionic gonadotropin},
  author={Adrian Jonathan Lapthorn and D. C. Harris and Allison Littlejohn and Joyce W. Lustbader and Robert E Canfield and K. J. Machin and F. J. Morgan and Neil W. Isaacs},
  journal={Nature},
  year={1994},
  volume={369},
  pages={455-461}
}
The three-dimensional structure of human chorionic gonadotropin shows that each of its two different subunits has a similar topology, with three disulphide bonds forming a cystine knot. This same folding motif is found in some protein growth factors. The heterodimer is stabilized by a segment of the β-subunit which wraps around the α-subunit and is covalently linked like a seat belt by the disulphide Cys 26–Cys 110. This extraordinary feature appears to be essential not only for the association… CONTINUE READING
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