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| Class:Id | Summation:982781 |
|---|---|
| _displayName | The growth hormone receptor (GHR) belongs to the superfamily... |
| _timestamp | 2011-06-24 09:08:57 |
| created | [InstanceEdit:982796] Jupe, S, 2010-10-28 |
| literatureReference | [LiteratureReference:1168346] Turning the growth hormone receptor on: evidence that hormone binding induces subunit rotation |
| modified | [InstanceEdit:1168344] Jupe, S, 2010-12-17 [InstanceEdit:1364048] Jupe, S, 2011-06-23 [InstanceEdit:1366608] Jupe, S, 2011-06-24 |
| text | The growth hormone receptor (GHR) belongs to the superfamily of transmembrane proteins that includes the prolactin receptor and a number of class 1 cytokine receptors. It exists in two forms, full-length membrane-bound receptor with a single transmembrane region, and growth hormone binding protein (GHBP), a shorter soluble form corresponding to the extracellular domain of the full-length receptor. In rodents GHBP is encoded by a specific mRNA variant while in humans it results from proteolytic cleavage of the membrane receptor by a metalloprotease. The classical view is that growth hormone sequentially binds 2 molecules of GHR inducing dimerization, but it is now widely accepted that GHR dimers exist prior to ligand binding (Poger & Mark 2010). |
| (summation) | [Reaction:982778] Growth hormone binds the growth hormone receptor [Homo sapiens] |
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