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.1994 Jun 9;369(6480):455-61.
doi: 10.1038/369455a0.

Crystal structure of human chorionic gonadotropin

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Crystal structure of human chorionic gonadotropin

A J Lapthorn et al. Nature..

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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