Sandbox Reserved 1779: Difference between revisions

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The thyrotropin receptor has an extracellular domain (ECD) that is composed of a <scene name='95/952709/Lrrd_real/2'>leucine rich repeat domain (LRRD)</scene> as well as a hinge region. This <scene name='95/952709/Hinge_region_real/2'>hinge region</scene> links the ECD to the seven transmembrane helices <scene name='95/952709/7tm_helices/4'>(7TM domain)</scene>, which span from the extracellular domain to the intracellular domain <ref name= "Keinau et al.">PMID:228484426</ref>. When thyrotropin or an autoantibody binds, it causes a conformational change in the receptor through the transmembrane helices. This causes the thyrotropin receptor to interact differently with its respective <scene name='95/952709/G_protein/2'>G-protein</scene> when in the active and inactive states.

=== Leucine Rich Region ===

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">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.

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 Lys58</scene> <ref name="Duan et al.">PMID: 35940204</ref>. These interact with <scene name='95/952709/Interactions_with_thyrotropin/1'>Glu 98 and Asp 91</scene> in the seatbelt region of TSH forming a salt bridge and initiating the conformational change in the receptor <ref name="Faust">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.

=== Active and Inactive Form ===

Sandbox Reserved 1779: Difference between revisions

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 The thyrotropin receptor has an extracellular domain (ECD) that is composed of a <scene name='95/952709/Lrrd_real/2'>leucine rich repeat domain (LRRD)</scene> as well as a hinge region. This <scene name='95/952709/Hinge_region_real/2'>hinge region</scene> links the ECD to the seven transmembrane helices <scene name='95/952709/7tm_helices/4'>(7TM domain)</scene>, which span from the extracellular domain to the intracellular domain <ref name= "Keinau et al.">PMID:228484426</ref>. When thyrotropin or an autoantibody binds, it causes a conformational change in the receptor through the transmembrane helices. This causes the thyrotropin receptor to interact differently with its respective <scene name='95/952709/G_protein/2'>G-protein</scene> when in the active and inactive states.
 === Leucine Rich Region ===
-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">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.
+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 Lys58</scene> <ref name="Duan et al.">PMID: 35940204</ref>. These interact with <scene name='95/952709/Interactions_with_thyrotropin/1'>Glu 98 and Asp 91</scene> in the seatbelt region of TSH forming a salt bridge and initiating the conformational change in the receptor <ref name="Faust">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.
 === Active and Inactive Form ===