Talk:Neurotensin receptor

From Proteopedia

Ideas for improvement

This "figure-review" was written by Meaghan Jones as part of an assignment for a Biochemistry course at Westfield State University, and posted here by the instructor with permission.

1. My favorite figure: Figure: “Trp321” in the Na⁺ Binding Pocket. The figure shows how the tryptophan 321 of the neurotensin receptor interacts with other molecules to control activity or inactivity of the neurotensin receptor. PDB Code: 4GRV and 4XEE Proteopedia script: https://proteopedia.org/wiki/scripts/72/721548/Trp321/1.spt. More supporting information was found at the two references below, with articles pertaining to the structure and function of the receptor. The primary citation is from 2009, and the link is: https://academic.oup.com/mend/article/24/1/261/2684236.
2. This is my suggestion for a figure legend: View of the NTSR1 (blue) where the tryptophan 321 of the neurotensin receptor works with Asp113 and four other molecules to dictate if the active site is active or inactive by determining if the tryptophan 321 of the neurotensin receptor is occluding the site.
3. What I like about the figure: It gives a representation of how the tryptophan 321 of the neurotensin receptor can regulate whether the NTS is in its active or inactive state. It also gives a good representation of where this regulation of active or inactive state is determined. It shows that the area that regulates this activity is right on top of the Na+ binding pocket.
4. Corresponding figure in the primary citation: Figure 2. It shows how the tryptophan 321 of the neurotensin receptor interacts to show a closed sodium binding pocket, which indicates that sodium ions are not entering the structure. It shows how the tryptophan 321 of the neurotensin receptor occludes the pocket.
5. How I think the figure could be improved: I think the figure could be improved by showing the Na+ binding pocket as a figure in the image instead of just labeling where the pocket would be with words. Where it is with words, it kind of looks like it is just pointing to thin air. I would also label which end of the structure is the intracellular and which is the extracellular part. It is hard to tell which way the molecule is because there is no labeling.

References

Millar RP, Newton CL. The year in G protein-coupled receptor research. Mol Endocrinol. 2010 Jan;24(1):261-74. Epub 2009 Dec 17. PMID:20019124 doi:10.1210/me.2009-0473

Fang Y, Lahiri J, Picard L. G protein-coupled receptor microarrays for drug discovery. Drug Discov Today. 2004 Dec 15;9(24 Suppl):S61-7. PMID:23573662

--Karsten Theis 19:31, 16 December 2018 (UTC)