http://purl.uniprot.org/citations/7922031 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/7922031 | http://www.w3.org/2000/01/rdf-schema#comment | "BackgroundHuman chorionic gonadotropin (hCG) is a placental hormone that stimulates secretion of the pregnancy-sustaining steroid progesterone. It is a member of a family of glycoprotein hormones that are disulfide-rich heterodimers, with a common alpha-chain and distinctive beta-chains specific to their particular G-protein linked receptors.ResultsWe have produced recombinant hCG in mammalian cells as the selenomethionyl protein, and have determined its structure (after partial deglycosylation) at 2.6 A resolution from multiwavelength anomalous diffraction (MAD) measurements. Despite only limited sequence similarity (10% identity), the alpha- and beta-subunits of hCG have similar tertiary folds. Each subunit has a cystine-knot motif at its core of extended hairpin loops. There is a very extensive subunit interface featuring two inter-chain beta-sheets and a unique, disulfide-tethered 'arm' from the beta-subunit which 'embraces' the alpha-subunit. The carboxy-terminal peptide of the beta-subunit, which is rich in O-linked sugars, is disordered.ConclusionsStructural and sequence comparisons indicate an evolutionary homology, albeit remote, between the glycoprotein hormone chains and other cystine-knot proteins, notably platelet-derived growth factor. Segments of the alpha- and beta-chains that have been convincingly implicated in receptor binding by hCG are juxtaposed on one side of the molecule. A glycosylation site implicated in signal transduction but not in binding is also close to the presumed binding site suggesting a possible coupling between ligand binding and signaling. This study with selenomethionyl protein produced in mammalian cells extends the realm of MAD phasing."xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0969-2126(00)00054-x"xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/author | "Wu H."xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/author | "Hendrickson W.A."xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/author | "Canfield R.E."xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/author | "Lustbader J.W."xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/pages | "545-558"xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/title | "Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein."xsd:string |
http://purl.uniprot.org/citations/7922031 | http://purl.uniprot.org/core/volume | "2"xsd:string |
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