Crystal structure of human chorionic gonadotropin
Copyright policy )Crystal structure of human chorionic gonadotropin
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.
- University of Glasgow United Kingdom
Models, Molecular, Protein Folding, Protein Conformation, Molecular Sequence Data, Receptors, LH, Crystallography, X-Ray, Chorionic Gonadotropin, Hormones, Carbohydrate Conformation, Computer Graphics, Cystine, Humans, Amino Acid Sequence, Disulfides, Growth Substances, Glycoproteins
Models, Molecular, Protein Folding, Protein Conformation, Molecular Sequence Data, Receptors, LH, Crystallography, X-Ray, Chorionic Gonadotropin, Hormones, Carbohydrate Conformation, Computer Graphics, Cystine, Humans, Amino Acid Sequence, Disulfides, Growth Substances, Glycoproteins
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