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http://purl.uniprot.org/citations/7984244http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7984244http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7984244http://www.w3.org/2000/01/rdf-schema#comment"The human pituitary hormones, growth hormone (hGH) and prolactin (hPRL), regulate a large variety of physiological processes, among which are growth and differentiation of muscle, bone and cartilage cells, and lactation. These activities are initiated by hormone-receptor binding. The hGH and hPRL receptors (hGHR and hPRLR, respectively) are single-pass transmembrane receptors from class 1 of the haematopoietic receptor superfamily. This classification is based on sequence similarity in their extracellular domains, notably a highly conserved pentapeptide, the so-called 'WSXWS box', the function of which is controversial. All ligands in class 1 activate their respective receptors by clustering mechanisms. In the case of hGH, activation involves receptor homodimerization in a sequential process: the active ternary complex containing one ligand and two receptor molecules is formed by association of a receptor molecule to an intermediate 1:1 complex. hPRL does not bind to the hGH receptor, but hGH binds to both the hGHR and hPRLR, and mutagenesis studies have shown that the receptor-binding sites on hGH overlap. We present here the crystal structure of the 1:1 complex of hGH bound to the extracellular domain of the hPRLR. Comparisons with the hGH-hGHR complex reveal how hGH can bind to the two distinctly different receptor binding surfaces."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.org/dc/terms/identifier"doi:10.1038/372478a0"xsd:string
http://purl.uniprot.org/citations/7984244http://purl.org/dc/terms/identifier"doi:10.1038/372478a0"xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/author"Kossiakoff A.A."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/author"Kossiakoff A.A."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/author"Somers W."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/author"Somers W."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/author"Ultsch M."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/author"Ultsch M."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/author"de Vos A.M."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/author"de Vos A.M."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/pages"478-481"xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/pages"478-481"xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/title"The X-ray structure of a growth hormone-prolactin receptor complex."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/title"The X-ray structure of a growth hormone-prolactin receptor complex."xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/volume"372"xsd:string
http://purl.uniprot.org/citations/7984244http://purl.uniprot.org/core/volume"372"xsd:string
http://purl.uniprot.org/citations/7984244http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7984244
http://purl.uniprot.org/citations/7984244http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7984244