Talk:Dipeptidyl peptidase IV
From Proteopedia
Ideas for improvement
This "figure-review" was written by Rachel Dunphy as part of an assignment for a Biochemistry course at Westfield State University, and posted here by the instructor with permission.
- My favorite figure: My favorite figure is when you click “Tyr547” on the Dipeptidyl Peptidase and it brings you to a detailed look at the active site. Here, we were able to see the catalytic triad, and its relationship with Tyrosine and Sitagliptin. The script can be found at : www.proteopedia.com/wiki/extensions/Proteopedia/spt/wipeFullLoadButton.spt; script /wiki/scripts/57/573132/1x70_activesitetyr/5.spt
- This is my suggestion for a figure: My suggestion is to have the distance between the Sitagliptin and the Serine, Histidine, and Alanine. It would give the viewer a better understanding of why the Tyrosine interacts more than the catalytic triad. I also suggest that the jsmol provided a little clearer way of seeing the active site while seeing the whole enzyme. I would like to see a differentiation between charged and nonpolar amino acids.
- What I like about the figure: What I like about the figure is that we are able to see Tyrosine, and its relationship to Sitagliptin, while also being able to see the catalytic triad. Also, it has how far away The tyrosine is from the substrate (4.08 angstroms). This closer look at the active site shows just how truly small it is- allowing usually only proline
- Corresponding figure in the primary citation: While none of the primary citations had figures, I was able to find “Dipeptdyl Peptidase” (http://proteopedia.org/wiki/index.php/Dipeptidyl_peptidase) that shows the interacton between he catalytic triad, and the substrate (with distances in Angstroms)
- How I think the figure could be improved: I think it would not only be good to have the distance between the different elements, but also to have the colors represent the charge/ polarity among the surrounding amino acids not in the active site. Here, the Tyrosine is shown to be 4.08 angstroms from the substrate, it would be nice to know how far that is in relation to the whole enzyme. I would like to also see the interaction between insulin and glucagon, since the figure legend mentioned its role.
References
Harel, M., Berchansky, A., Sussman, J. (2018). Dipeptidyl Peptidase. Proteopedia. Received from: http://proteopedia.org/wiki/index.php/Dipeptidyl_peptidase
Green BD, Flatt PR, Bailey CJ. Dipeptidyl peptidase IV (DPP IV) inhibitors: A newly emerging drug class for the treatment of type 2 diabetes. Diab Vasc Dis Res. 2006 Dec;3(3):159-65. PMID:17160910doi:http://dx.doi.org/10.3132/dvdr.2006.024
--Karsten Theis 03:43, 17 December 2018 (UTC)