Sandbox Reserved 1791: Difference between revisions

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[[Image:Image-Inactive Inactive Proteopedia.png|300 px|right|thumb| Figure 2: An overview of the Inactive (red) vs Active (green) state of TSHR. PDB: 7WX5]]
[[Image:Image-Inactive Inactive Proteopedia.png|300 px|right|thumb| Figure 2: An overview of the Inactive (red) vs Active (green) state of TSHR. PDB: 7WX5]]
[[Image:Inactive v active residue.png|300 px|right|thumb| Figure 3: A zoomed in view of the Y279 residue in the Hinge Region of TSHR, showing the 6 angstrom move of Y279 during the activation of TSHR. Active TSHR is shown in green (PDB: 7t9i) and inactive TSHR is shown in pink (PDB: 7t9m).]]
[[Image:Inactive v active residue.png|300 px|right|thumb| Figure 3: A zoomed in view of the Y279 residue in the Hinge Region of TSHR, showing the 6 angstrom move of Y279 during the activation of TSHR. Active TSHR is shown in green (PDB: 7t9i) and inactive TSHR is shown in pink (PDB: 7t9m).]]
In its resting state without TSH, TSHR is in the <scene name='95/952720/Inactivetshr/7'>inactive state</scene>, also considered the "down" state because the LRRD is pointing down. When TSH binds to TSHR, steric clashes between TSH and the cell-membrane cause TSHR to take on the <scene name='95/952720/Inactivetshr/6'>active or "up" state</scene>. During this transition, the extracellular LRD rotates 55° along an axis making it perpendicular to the cell membrane. This rotation is initiated by conformational changes within the <scene name='95/952720/Hinge_region_spin/3'>Hinge Region</scene>, specifically at the <scene name='95/952720/Hinge_region_residues/2'>TYR279 residue</scene>. Y279 moves 6 Å relative to I486, a residue located in the Transmembrane Region <ref name="Faust"/>. The active form is favored when <scene name='95/952719/Active_form/6'>TSHR is bound to TSH</scene>. The structure can be seen as straight. The same straight conformation is observed when TSHR is bound with M22. The inactive form is found when <scene name='95/952719/Inactive_form/7'>TSHR is bound with K1</scene> of TSHR is found when bound with K1. The overall structure of the molecule is bent when K1 is bound.  
In its resting state without TSH, TSHR is in the <scene name='95/952720/Inactivetshr/7'>inactive state</scene>, also considered the "down" state because the LRRD is pointing down. When TSH binds to TSHR, steric clashes between TSH and the cell-membrane cause TSHR to take on the <scene name='95/952720/Inactivetshr/6'>active or "up" state</scene>. During this transition, the extracellular LRD rotates 55° along an axis making it perpendicular to the cell membrane. This rotation is initiated by conformational changes within the <scene name='95/952720/Hinge_region_spin/3'>Hinge Region</scene>, specifically at the <scene name='95/952720/Hinge_region_residues/2'>TYR279 residue</scene>. Y279 moves 6 Å relative to I486, a residue located in the Transmembrane Region <ref name="Faust"/>. The active form is favored when <scene name='95/952719/Active_form/7'>TSHR is bound to TSH</scene>. The structure can be seen as straight. The same straight conformation is observed when TSHR is bound with M22. The inactive form is found when <scene name='95/952719/Inactive_form/8'>TSHR is bound with K1</scene> of TSHR is found when bound with K1. The overall structure of the molecule is bent when K1 is bound.  
<scene name='95/952719/Active_form/5'>TextToBeDisplayed</scene>
<scene name='95/952719/Active_form/5'>TextToBeDisplayed</scene>
== Specific Residues and Interactions==
== Specific Residues and Interactions==