doi: 10.1038/369455a0.
Crystal structure of human chorionic gonadotropin
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- PMID: 8202136
- DOI: 10.1038/369455a0
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Crystal structure of human chorionic gonadotropin
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.
Comment in
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Glycoprotein hormones. A clasped embrace.Nature. 1994 Jun 9;369(6480):438-9. doi: 10.1038/369438a0. Nature. 1994. PMID: 8202130 No abstract available.
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