| http://purl.uniprot.org/citations/8943276 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8943276 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8943276 | http://www.w3.org/2000/01/rdf-schema#comment | "Human growth hormone binds two receptor molecules and thereby induces signal transduction through receptor dimerization. At high concentrations, growth hormone acts as an antagonist because of a large difference in affinities at the respective binding sites. This antagonist action can be enhanced further by reducing binding in the low affinity binding site. A growth hormone antagonist mutant Gly-120 --> Arg, has been crystallized with its receptor as a 1:1 complex and the crystal structure determined at 2.9 A resolution. The 1:1 complex is remarkably similar to the native growth hormone-receptor 1:2 complex. A comparison between the two structures reveals only minimal differences in the conformations of the hormone or its receptor in the two complexes, including the angle between the two immunoglobulin-like domains of the receptor. Further, two symmetry-related 1:1 complexes in the crystal form a 2:2 complex with a large solvent inaccessible area between two receptor molecules. In addition, we present here a native human growth hormone-human growth hormone-binding protein 1:2 complex structure at 2.5 A resolution. One important difference between our structure and the previously published crystal structure at 2.8 A is revealed. Trp-104 in the receptor, a key residue in the hormone-receptor interaction, has an altered conformation in the low affinity site enabling a favorable hydrogen bond to be formed with Asp-116 of the hormone."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.271.50.32197"xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.271.50.32197"xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Roedin J."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Roedin J."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Sundstroem M."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Sundstroem M."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Lundqvist T."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Lundqvist T."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Giebel L.B."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Giebel L.B."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Milligan D."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Milligan D."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Norstedt G."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/author | "Norstedt G."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/pages | "32197-32203"xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/pages | "32197-32203"xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/title | "Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9-A resolution."xsd:string |
| http://purl.uniprot.org/citations/8943276 | http://purl.uniprot.org/core/title | "Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9-A resolution."xsd:string |