2N7I
NMR structure of the prolactin receptor transmembrane domain
Summary for 2N7I
| Entry DOI | 10.2210/pdb2n7i/pdb |
| NMR Information | BMRB: 25806 |
| Descriptor | Prolactin receptor (1 entity in total) |
| Functional Keywords | transmembrane domain, membrane protein, receptor, hormone receptor |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane ; Single-pass type I membrane protein . Isoform 7: Secreted: P16471 |
| Total number of polymer chains | 1 |
| Total formula weight | 3960.74 |
| Authors | Bugge, K.,Kragelund, B.B. (deposition date: 2015-09-11, release date: 2016-05-18, Last modification date: 2024-05-15) |
| Primary citation | Bugge, K.,Papaleo, E.,Haxholm, G.W.,Hopper, J.T.,Robinson, C.V.,Olsen, J.G.,Lindorff-Larsen, K.,Kragelund, B.B. A combined computational and structural model of the full-length human prolactin receptor. Nat Commun, 7:11578-11578, 2016 Cited by PubMed Abstract: The prolactin receptor is an archetype member of the class I cytokine receptor family, comprising receptors with fundamental functions in biology as well as key drug targets. Structurally, each of these receptors represent an intriguing diversity, providing an exceptionally challenging target for structural biology. Here, we access the molecular architecture of the monomeric human prolactin receptor by combining experimental and computational efforts. We solve the NMR structure of its transmembrane domain in micelles and collect structural data on overlapping fragments of the receptor with small-angle X-ray scattering, native mass spectrometry and NMR spectroscopy. Along with previously published data, these are integrated by molecular modelling to generate a full receptor structure. The result provides the first full view of a class I cytokine receptor, exemplifying the architecture of more than 40 different receptor chains, and reveals that the extracellular domain is merely the tip of a molecular iceberg. PubMed: 27174498DOI: 10.1038/ncomms11578 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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