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Sandbox Reserved 1791

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Revision as of 17:43, 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

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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

The binding pocket allows a tight interaction with the antibodies. These antibodies make tight interactions with a lot of IMFs at play.
Specifically the two residues make an ionic interaction. The interaction is not close enough to make a hydrogen bond. Instead, the interaction between the Lys residues with the Asp or Glu residues is a salt bridge interaction. This is the main bond that holds these two molecules together.

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"

@@ Line 35: / Line 35: @@
 *<scene name='95/952719/Specific_residues/3'>LYS w/ label</scene>
 === Interactions ===
-*<scene name='95/952719/Lock_and_key/1'>Tight interaction</scene>
+*The binding pocket allows a tight interaction with the antibodies. These antibodies make tight interactions with a lot of IMFs at play. <scene name='95/952719/Lock_and_key/1'>Tight interaction</scene>
-*<scene name='95/952719/K---d_interaction/1'>LYS ASP interaction</scene>
+*Specifically the two residues make an ionic interaction. The interaction is not close enough to make a hydrogen bond. Instead, the interaction between the Lys residues with the Asp or Glu residues is a salt bridge interaction. This is the main bond that holds these two molecules together. <scene name='95/952719/K---d_interaction/1'>LYS ASP interaction</scene>
 *<scene name='95/952719/K---e_interaction/1'>LYS GLU interaction</scene>
 == Biological Relevance ==