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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6480
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pubmed:dateCreated |
1994-7-5
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pubmed:abstractText |
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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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
369
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
455-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8202136-Amino Acid Sequence,
pubmed-meshheading:8202136-Carbohydrate Conformation,
pubmed-meshheading:8202136-Chorionic Gonadotropin,
pubmed-meshheading:8202136-Computer Graphics,
pubmed-meshheading:8202136-Crystallography, X-Ray,
pubmed-meshheading:8202136-Cystine,
pubmed-meshheading:8202136-Disulfides,
pubmed-meshheading:8202136-Glycoproteins,
pubmed-meshheading:8202136-Growth Substances,
pubmed-meshheading:8202136-Hormones,
pubmed-meshheading:8202136-Humans,
pubmed-meshheading:8202136-Models, Molecular,
pubmed-meshheading:8202136-Molecular Sequence Data,
pubmed-meshheading:8202136-Protein Conformation,
pubmed-meshheading:8202136-Protein Folding,
pubmed-meshheading:8202136-Receptors, LH
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pubmed:year |
1994
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pubmed:articleTitle |
Crystal structure of human chorionic gonadotropin.
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pubmed:affiliation |
Department of Chemistry, University of Glasgow, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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