User:Brynn Baker/Sandbox1

From Proteopedia

(Difference between revisions)

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 == Amylin ==
 Amylin is a neuroendocrine hormone that is synthesized with insulin in the [https://en.wikipedia.org/wiki/Beta_cell beta cells] of pancreatic islets. It can cross the [https://en.wikipedia.org/wiki/Blood%E2%80%93brain_barrier blood-brain barrier] and regulates glucose homeostasis via inhibiting gastric emptying, inhibiting the release of glucagon, and inducing meal-ending satiety. In doing so, it prevents spikes in blood glucose and overeating, making it a suitable target for [https://en.wikipedia.org/wiki/Type_2_diabetes Type 2 Diabetes]. Type 2 Diabetes treatments and therapies. Seeing as Type 2 Diabetes is a major risk factor for [https://en.wikipedia.org/wiki/Alzheimer%27s_disease Alzheimer's Disease], as Type 2 Diabetes cases continue to increase, there will likely be a spike in Alzheimer’s Disease as well. Therefore, it is vital that amylin, its receptor, and analogs such as pramlintide are understood to aid in rational drug design.
-=== Amidated C-Terminus ===
+=== Structure ===
-== G-Coupled Protein Receptor Interactions ==
+== Amylin Receptor ==
+The amylin receptor (AMYR) is the result of the heterodimerization of the calcitonin receptor (CT) and a receptor-activity modifying protein (RAMP). The patterns of peptide interaction between CT and AMYR are very similar overall, but amylin has a higher affinity for AMYR1 and AMYR3 than AMYR2.
+== Calcitonin Receptor and G-alpha Interactions ==
 == RAMPs ==
+=== Amylin Binding ===
 == Amylin Receptor Functional Overview ==
-<scene name='10/1037520/Brynn_first_scene/4'>Chain R Overview</scene>
+=== Hydrophobic Interactions ===
-=== Key Interactions ===
+The tyrosine on the C-terminus of the amylin peptide has extensive van der Waals interactions with the CT and RAMP3. The pi stacking and hydrophobic interactions increase the affinity and interactions between the amylin peptide, CT, and RAMP3, aiding in their association.
-The <scene name='10/1037520/Hydrophobic_pocket/1'>hydrophobic pocket</scene> aids in amylin affinity and the formation of the AMYR3.
+=== Amidated C-Terminus ===
-The <scene name='10/1037520/Amidated_cterm/1'>amidated c-terminus</scene> of the amylin is a very interesting mutation.
+=== R11 ===
+=== R18 ===
+=== T9 Water Network ===
 == Disease ==

Revision as of 19:24, 9 April 2024

Homo sapiens Amylin3 Receptor, AMYR3

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Human Amylin3 Receptor, 7TZF

Show:Asymmetric Unit Biological Assembly

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This is a default text for your page Brynn Baker/Sandbox1. 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 Amylin
- 2.1 Structure
3 Amylin Receptor
4 Calcitonin Receptor and G-alpha Interactions
5 RAMPs
- 5.1 Amylin Binding
6 Amylin Receptor Functional Overview
7 Disease
8 Relevance
9 Structural highlights

Introduction

Figure 1. The coolest image of this protein EVAH!!!

The human amylin receptor is a G-coupled protein receptor.

Amylin

Amylin is a neuroendocrine hormone that is synthesized with insulin in the beta cells of pancreatic islets. It can cross the blood-brain barrier and regulates glucose homeostasis via inhibiting gastric emptying, inhibiting the release of glucagon, and inducing meal-ending satiety. In doing so, it prevents spikes in blood glucose and overeating, making it a suitable target for Type 2 Diabetes. Type 2 Diabetes treatments and therapies. Seeing as Type 2 Diabetes is a major risk factor for Alzheimer's Disease, as Type 2 Diabetes cases continue to increase, there will likely be a spike in Alzheimer’s Disease as well. Therefore, it is vital that amylin, its receptor, and analogs such as pramlintide are understood to aid in rational drug design.

Structure

Amylin Receptor

The amylin receptor (AMYR) is the result of the heterodimerization of the calcitonin receptor (CT) and a receptor-activity modifying protein (RAMP). The patterns of peptide interaction between CT and AMYR are very similar overall, but amylin has a higher affinity for AMYR1 and AMYR3 than AMYR2.

Calcitonin Receptor and G-alpha Interactions

RAMPs

Amylin Binding

Amylin Receptor Functional Overview

Hydrophobic Interactions

The tyrosine on the C-terminus of the amylin peptide has extensive van der Waals interactions with the CT and RAMP3. The pi stacking and hydrophobic interactions increase the affinity and interactions between the amylin peptide, CT, and RAMP3, aiding in their association.

Amidated C-Terminus

R11

R18

T9 Water Network

Disease

Pramlintide Analogue

Type 2 Diabetes

Alzheimer's Disease

The proline mutations can help prevent disease. ^[3]

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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
↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677

Student Contributors

Brynn Baker
Emily Berkman
Sepp Hall

Proteopedia Page Contributors and Editors (what is this?)

Brynn Baker

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