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Revision as of 03:11, 19 April 2016

Figure Legend

NTSR1-ELF, Rattus norvegicus

An interactive view of the class A GPCR, NTSR1, which is shown in blue. This protein gets its activity from binding to its 13 amino acid ligand, NTS, which is shown in red.

Drag the structure with the mouse to rotate

This is a default text for your page Danny Cotter/Sandbox 1. 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 Pymol Pictures
- 2.1 Na+ Binding Pocket
3 Neurotensin (Ligand)
4 Function
5 Disease
6 Relevance
7 Structural highlights

Introduction

Neurotensin receptor 1 (NTSR1) is a G-protein coupled receptor (GPCR) that binds to the 13 amino acid peptide, neurotensin. Studies determining the structure of NTSR1 crystallized the GPCR bound with the C-terminus of its tridecapeptide ligand, because it has a higher potency and efficacy than its full-length counterpart. NTSR1 is a class A GPCR, and like all G-proteins, consists of an extracellular binding domain along with 7 transmembrane helices. Along with the ligand binding pocket at the top of the protein, NTSR1 also contains an allosteric Na+ ion binding pocket underneath. NTS binds to NTSR1, leading to a conformational change of the protein and modulation of second messengers. NTS has been shown to have a variety of biological activities including a role in the leptin signalling pathways, tumor growth, and dopamine regulation. The majority of effects of NTS are mediated through NTSR1. Research of the structure of NTSR1 has focused on the differences between its active and active-like states.

Pymol Pictures

Na+ Binding Pocket

, which is positioned at the bottom of the hydrophobic pocket(green link from allie), sets the top of the . The Na+ ion binding pocket acts as a negative allosteric site for G protein activity. When Na+ enters the Na+ ion binding pocket, it coordinates with Asp95, Gln131, and S135, and shuts down the activity of the protein. When the G protein is in its active state, the Na+ ion binding pocket is collapsed, preventing the regulation of protein activity through a Na+ ion. In this case, the Na+ ion is coordinated by a salt bridge to Asp113. The side chain atoms of Asp113 form a hydrogen bond network with Thr156, Ser361, Ser362, and Gln365, which prevents the coordination of a Na+ ion.

Neurotensin (Ligand)

Function

Disease

Relevance

Structural highlights

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

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 == Structural highlights ==
-This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
+<scene name='72/721548/L310/2'>TextToBeDisplayed</scene>
 </StructureSection>
 == References ==
 <references/>

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From Proteopedia

Revision as of 03:11, 19 April 2016

NTSR1-ELF, Rattus norvegicus

Contents

Introduction

Pymol Pictures

Na+ Binding Pocket

Neurotensin (Ligand)

Function

Disease

Relevance

Structural highlights

References

Views

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