Crystal structure of human chorionic gonadotropin

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carbohydrate Conformation
  • Chorionic Gonadotropin / chemistry*
  • Chorionic Gonadotropin / metabolism
  • Computer Graphics
  • Crystallography, X-Ray
  • Cystine / chemistry
  • Disulfides / chemistry
  • Glycoproteins / chemistry
  • Growth Substances / chemistry
  • Hormones / chemistry
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Receptors, LH / metabolism


  • Chorionic Gonadotropin
  • Disulfides
  • Glycoproteins
  • Growth Substances
  • Hormones
  • Receptors, LH
  • Cystine