PROSITE documentation PDOC00234Glycoprotein hormones beta chain signatures
Glycoprotein hormones [1,2] (or gonadotropins) are a family of proteins which include the mammalian hormones follitropin (FSH), lutropin (LSH), thyrotropin (TSH) and chorionic gonadotropin (CG), as well as at least two forms of fish gonadotropins. All these hormones consist of two glycosylated chains (α and β). In mammalian gonadotropins, the α chain is identical in the four types of hormones but the β chains, while homologous, are different.
The β chains are proteins of about 100 to 140 amino acid residues which contain twelve conserved cysteines all involved in disulfide bonds [3], as shown in the following schematic representation.
+----------------------+ | +------------|-----------------------------+ | +-|------------|--------+ | | | | **** | | *************** xxxCxxxxxxxCxCxxCxCxxxxxxxCxxxxxxxxCxxxxxxxCxCxCxxCxxxxxCxxxxxxxxxxx | | | | | | | | | | +--+ +-|------------------------+ | +--------------------------+
'C': conserved cysteine involved in a disulfide bond. '*': position of the patterns.
We have developed two patterns for these hormones. The first one, located in the N-terminal section, is a region which has been said to be involved in the association between the two chains of the hormones. The second pattern consists of a cluster of five conserved cysteines in the C-terminal section.
Expert(s) to contact by email: Last update:April 2006 / Pattern revised.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Pierce J.G. Parsons T.F. |
Title | Glycoprotein hormones: structure and function. | |
Source | Annu. Rev. Biochem. 50:465-495(1981). | |
PubMed ID | 6267989 |
2 | Authors | Stockell Hartree A. Renwick A.G.C. |
Source | Biochem. J. 287:665-679(1992). |
3 | Authors | Lapthorn A.J. Harris D.C. Littlejohn A. Lustbader J.W. Canfield R.E. Machin K.J. Morgan F.J. Isaacs N.W. |
Title | Crystal structure of human chorionic gonadotropin. | |
Source | Nature 369:455-461(1994). | |
PubMed ID | 8202136 | |
DOI | 10.1038/369455a0 |
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