Sandbox Reserved 1780: Difference between revisions

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=== Active and Inactive Form ===

[[Image:Morphmembrane.png|450 px|right|thumb|Figure 2: Inactive form of the thyrotropin receptor shown in blue (PDB: 7T9M). Active form of the thyrotropin receptor shown in green (PDB: 7T9I).]]

The TSHR protein exists in two states: active and inactive (Figure 2) (GREEN LINK ?). The <scene name='95/952708/Tshr_chainr/4'>TSHR active form</scene> (GREEN LINK take away extra molecules) exists in dynamic equilibrium where <scene name='95/952708/Tsh_7t9i/1'>TSH</scene> (GREEN LINK make TSH one color) binding favors the active state. In this active state, TSH will bind and keep the active state in the up position because of clashes between bound TSH and the cell membrane.<ref name="Faust" />. Glycosylations of an Asn52 cause this clash on the <scene name='95/952707/Tsh_7t9i/1'>α-subunit of TSH</scene>. The addition of N-acetyl glucosamine modifications creates steric clashes between TSH and the cell membrane, keeping TSHR in the active state.

The TSHR protein exists in two states: active and inactive (Figure 2) (GREEN LINK ?). The <scene name='95/952708/Tshr_chainr/4'>TSHR active form</scene> (GREEN LINK take away extra molecules) exists in dynamic equilibrium where <scene name='95/952708/Tsh_7t9i/1'>TSH</scene> (GREEN LINK make TSH one color) binding favors the active state. In this active state, TSH will bind and keep the active state in the up position because of clashes between bound TSH and the cell membrane.<ref name="Faust" />. Glycosylations of an Asn52 cause this clash (GREEN LINK) on the <scene name='95/952707/Tsh_7t9i/1'>α-subunit of TSH</scene>. The addition of N-acetyl glucosamine modifications creates steric clashes between TSH and the cell membrane, keeping TSHR in the active state.

== TSHR Agonists and Antagonists ==

Sandbox Reserved 1780: Difference between revisions

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@@ Line 5: / Line 5: @@
 === Active and Inactive Form ===
 [[Image:Morphmembrane.png|450 px|right|thumb|Figure 2: Inactive form of the thyrotropin receptor shown in blue (PDB: 7T9M). Active form of the thyrotropin receptor shown in green (PDB: 7T9I).]]
-The TSHR protein exists in two states: active and inactive (Figure 2) (GREEN LINK ?). The <scene name='95/952708/Tshr_chainr/4'>TSHR active form</scene> (GREEN LINK take away extra molecules) exists in dynamic equilibrium where <scene name='95/952708/Tsh_7t9i/1'>TSH</scene> (GREEN LINK make TSH one color) binding favors the active state. In this active state, TSH will bind and keep the active state in the up position because of clashes between bound TSH and the cell membrane.<ref name="Faust" />. Glycosylations of an Asn52 cause this clash on the <scene name='95/952707/Tsh_7t9i/1'>α-subunit of TSH</scene>. The addition of N-acetyl glucosamine modifications creates steric clashes between TSH and the cell membrane, keeping TSHR in the active state.
+The TSHR protein exists in two states: active and inactive (Figure 2) (GREEN LINK ?). The <scene name='95/952708/Tshr_chainr/4'>TSHR active form</scene> (GREEN LINK take away extra molecules) exists in dynamic equilibrium where <scene name='95/952708/Tsh_7t9i/1'>TSH</scene> (GREEN LINK make TSH one color) binding favors the active state. In this active state, TSH will bind and keep the active state in the up position because of clashes between bound TSH and the cell membrane.<ref name="Faust" />. Glycosylations of an Asn52 cause this clash (GREEN LINK) on the <scene name='95/952707/Tsh_7t9i/1'>α-subunit of TSH</scene>. The addition of N-acetyl glucosamine modifications creates steric clashes between TSH and the cell membrane, keeping TSHR in the active state.
 == TSHR Agonists and Antagonists ==