Sandbox Reserved 1646

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=== General structure ===
=== General structure ===
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GnRH1R has the overall architecture of seven canonical transmembrane (TM) helices with connecting extra- and intracellular loop domains (ECL/ICL) similar to [https://en.wikipedia.org/wiki/Rhodopsin-like_receptors rhodopsin like receptors]. However, it lacks the typically occurring cytoplasmic C-terminal helix and has an unusual ligand binding mode. The structural variation between existing GnRHR Typ I, II and III in different species has been analyzed <ref>DOI: 10.1210/er.2003-0002</ref>. First crystallographic structure analysis of human GnGH1R serve the investigation of the molecular mechanism of the receptor <ref> DOI: 10.1038/s41467-020-19109-w>. In this analysis the GnRH1R contains certain modifications: ICL3 (aa 243-256) is replaced by the Pyrococcus abysi glycogen synthase (22), it is in a complex with the antagonistic drug elagolix, and remains in inactive conformation in respect to G protein coupling.
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GnRH1R has the overall architecture of seven canonical transmembrane (TM) helices with connecting extra- and intracellular loop domains (ECL/ICL) similar to [https://en.wikipedia.org/wiki/Rhodopsin-like_receptors rhodopsin like receptors]. However, it lacks the typically occurring cytoplasmic C-terminal helix and has an unusual ligand binding mode. The structural variation between existing GnRHR Typ I, II and III in different species has been analyzed <ref>DOI: 10.1210/er.2003-0002</ref>. First crystallographic structure analysis of human GnGH1R serve the investigation of the molecular mechanism of the receptor. In this analysis the GnRH1R contains certain modifications: ICL3 (aa 243-256) is replaced by the Pyrococcus abysi glycogen synthase (22), it is in a complex with the antagonistic drug elagolix, and remains in inactive conformation in respect to G protein coupling.
In this conformation, an intrahelical salt bridge is observed between D1383.49 and R1393.50, as well as a polar interaction between R139 3.50 and T265 6.33 (This restricts the outward movement of those TMs associated with GPCR activation).
In this conformation, an intrahelical salt bridge is observed between D1383.49 and R1393.50, as well as a polar interaction between R139 3.50 and T265 6.33 (This restricts the outward movement of those TMs associated with GPCR activation).
The ECL2 of GnRH1R forms an extended β-hairpin and is anchored to the extracellular tip of TM3 through a conserved disulfide bond between residues C1143.25 and C196 in ECL2.
The ECL2 of GnRH1R forms an extended β-hairpin and is anchored to the extracellular tip of TM3 through a conserved disulfide bond between residues C1143.25 and C196 in ECL2.

Revision as of 06:29, 23 January 2021

This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664.
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Gonadotropin releasing hormone 1 receptor (GnRHR)

PDB ID 7BR3

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