Sandbox Reserved 1779

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== Leucine Rich Region ==
== Leucine Rich Region ==
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The Leucine Rich region is part of the <scene name='95/952708/Tshr_chainr_ecd/1'>extracellular domain (ECD)</scene> of TSHR. The highlighted region contains 10-11 Leucine repeats within the structure. The specific residues from TSHR interacting with TSH are <scene name='95/952707/Lrr/2'>Lys209 and Lys 58</scene> <ref name="Duan et al.">PMID: 35940204</ref>. These interact with Asp91 and Glu98 in the seatbelt region of TSH forming a salt bridge and initiating the conformational change in the receptor <ref name="Faust et al.">PMID: 35940205</ref>. This interaction is specific to TSH and TSHR. When other agonists or antagonists bind to the receptor, the interaction is a result of different residues interacting. The Leucine residues likely play a role in how the ECD folds and which residues are located on the exterior protein. As Leucine is hydrophobic, it would be forced into the interior of the protein during folding exposing other residues that are more hydrophobic to the surface.
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The Leucine Rich region is part of the <scene name='95/952708/Tshr_chainr_ecd/1'>extracellular domain (ECD)</scene> of TSHR. The highlighted region contains <scene name='95/952707/Lrr/3'>10-11 Leucine Repeats</scene> within the structure. The specific residues from TSHR interacting with TSH are <scene name='95/952707/Lrr/2'>Lys209 and Lys 58</scene> <ref name="Duan et al.">PMID: 35940204</ref>. These interact with Asp91 and Glu98 in the seatbelt region of TSH forming a salt bridge and initiating the conformational change in the receptor <ref name="Faust et al.">PMID: 35940205</ref>. This interaction is specific to TSH and TSHR. When other agonists or antagonists bind to the receptor, the interaction is a result of different residues interacting. The Leucine residues likely play a role in how the ECD folds and which residues are located on the exterior protein. As Leucine is hydrophobic, it would be forced into the interior of the protein during folding exposing other residues that are more hydrophobic to the surface.

Revision as of 21:04, 27 March 2023

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This Sandbox is Reserved from February 27 through August 31, 2023 for use in the course CH462 Biochemistry II taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1765 through Sandbox Reserved 1795.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Thyrotropin Receptor 7T9M

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References

  1. ↑ Duan J, Xu P, Luan X, Ji Y, He X, Song N, Yuan Q, Jin Y, Cheng X, Jiang H, Zheng J, Zhang S, Jiang Y, Xu HE. Hormone- and antibody-mediated activation of the thyrotropin receptor. Nature. 2022 Aug 8. pii: 10.1038/s41586-022-05173-3. doi:, 10.1038/s41586-022-05173-3. PMID:35940204 doi:http://dx.doi.org/10.1038/s41586-022-05173-3
  2. ↑ Faust B, Billesbolle CB, Suomivuori CM, Singh I, Zhang K, Hoppe N, Pinto AFM, Diedrich JK, Muftuoglu Y, Szkudlinski MW, Saghatelian A, Dror RO, Cheng Y, Manglik A. Autoantibody mimicry of hormone action at the thyrotropin receptor. Nature. 2022 Aug 8. pii: 10.1038/s41586-022-05159-1. doi:, 10.1038/s41586-022-05159-1. PMID:35940205 doi:http://dx.doi.org/10.1038/s41586-022-05159-1
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