Sandbox Reserved 1779: Difference between revisions

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=== Leucine Rich Region ===

The Leucine Rich region (LRRD) is part of the <scene name='95/952708/Tshr_chainr_ecd/1'>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'>K209 and K58</scene> <ref name="Duan et al.">PMID: 35940204</ref>. These interact with <scene name='95/~~952709~~/Interactions_with_thyrotropin/1'> E98 ~~and N91~~</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 change in conformation 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 hydrophilic and likely to interact externally.

The Leucine Rich region (LRRD) is part of the <scene name='95/952708/Tshr_chainr_ecd/1'>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'>K209 and K58</scene> <ref name="Duan et al.">PMID: 35940204</ref>. These interact with <scene name='95/952707/Interactions_with_thyrotropin/2'>N91 and E98</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 change in conformation 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 hydrophilic and likely to interact externally.

===Hinge Region and P10 Peptide===

Sandbox Reserved 1779: Difference between revisions

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@@ Line 17: / Line 17: @@
 === Leucine Rich Region ===
-The Leucine Rich region (LRRD) is part of the <scene name='95/952708/Tshr_chainr_ecd/1'>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'>K209 and K58</scene> <ref name="Duan et al.">PMID: 35940204</ref>. These interact with <scene name='95/952709/Interactions_with_thyrotropin/1'> E98 and N91</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 change in conformation 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 hydrophilic and likely to interact externally.
+The Leucine Rich region (LRRD) is part of the <scene name='95/952708/Tshr_chainr_ecd/1'>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'>K209 and K58</scene> <ref name="Duan et al.">PMID: 35940204</ref>. These interact with <scene name='95/952707/Interactions_with_thyrotropin/2'>N91 and E98</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 change in conformation 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 hydrophilic and likely to interact externally.
 ===Hinge Region and P10 Peptide===