Crystal structure of human chorionic gonadotropin.

Abstract

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 beta-subunit which wraps around the alpha-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 of these heterodimers but also for receptor binding by the glycoprotein hormones.

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@article{Lapthorn1994CrystalSO, title={Crystal structure of human chorionic gonadotropin.}, author={Adrian Jonathan Lapthorn and Donnie C Harris and Alaina Littlejohn and Joyce W Lustbader and Robert E. Canfield and K J Machin and Fraser J. Morgan and Neil W. Isaacs}, journal={Nature}, year={1994}, volume={369 6480}, pages={455-61} }