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Sandbox Reserved 1791

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Revision as of 17:40, 24 March 2023

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.

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Thyrotropin Receptor

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Introduction
2 Structure
3 Active vs. Inactive State
4 Specific Residues
- 4.1 Interactions
5 Biological Relevance

Introduction

Thyroid Stimulating Hormone Receptor (TSHR) is a type of G-Protein Coupled Receptor (GPCR) found in human thyroid follicles. It is activated by the Thyroid Stimulating Hormone (TSH) which is known as thyrotropin. Activation of TSHR is necessary for activating a signaling pathway for the production of thyroid hormones such as T3 and T4

An overview of the Thyroid System source: Thyroid Hormones

Structure

: Leucine Rich Region Domain (coral), the hinge region (blue-purple), and the transmembrane region. The (rainbow). The leucine rich region domain is located on the outside of the cell. This is where TSH will bind. The hinge region is also extracellular. Conformational changes in this region are responsible for the switch between the active vs inactive state.

Transmembrane Region

()

Hinge Region

Leucine Rich Domain

Binding Pocket

a concave structure with many polar residues

Active vs. Inactive State

The active form of TSHR is found when bound by TSH or M22. The structure can be seen as straight.
The inactive form of TSHR is found when bound with K1. The overall structure of the molecule when K1 is bound is bent.

Specific Residues

LYS 58 interacts with Glu 118 on each of the antibodies
LYS 209 interacts with Asp 11 on each of the antibodies
When in the inactive form, Lys 209 does not interact with any residue but Lys 58 has interaction with Glu 118 and this interaction pulls the molecule into the bent position.

Interactions

Biological Relevance

References

↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Student Contributions

Alex Kem
Grace Lane

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1791"

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-<scene name='95/952719/Binding_pocket/2'>Binding Pocket1</scene>
+{{Template:CH462_Biochemistry_II_2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
-<scene name='95/952719/Tshr_unfinished/1'>Text To Be Displayed</scene>{{Template:CH462_Biochemistry_II_2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
 ==Thyrotropin Receptor==
 <StructureSection load='7xw5' size='340' side='right' caption='Caption for this structure' scene=''>
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 === Binding Pocket===
 <scene name='95/952719/Binding_pocket/2'>Binding Pocket</scene>
+*a concave structure with many polar residues
 == Active vs. Inactive State ==
-*<scene name='95/952719/Active_form/2'>Active Form</scene>
+*The active form of TSHR is found when bound by TSH or M22. The structure can be seen as straight. <scene name='95/952719/Active_form/2'>Active Form</scene>
-*<scene name='95/952719/Inactive_form/2'>Inactive form</scene>
+*The inactive form of TSHR is found when bound with K1. The overall structure of the molecule when K1 is bound is bent. <scene name='95/952719/Inactive_form/2'>Inactive form</scene>
 == Specific Residues ==
+*LYS 58 interacts with Glu 118 on each of the antibodies
+*LYS 209 interacts with Asp 11 on each of the antibodies
+*When in the inactive form, Lys 209 does not interact with any residue but Lys 58 has interaction with Glu 118 and this interaction pulls the molecule into the bent position.
 *<scene name='95/952719/Specific_residues/1'>LYS Residues</scene>
 *<scene name='95/952719/Specific_residues/2'>LYS closer look</scene>