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User:Sam Magnabosco/Sandbox1
From Proteopedia
< User:Sam Magnabosco(Difference between revisions)
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=Sam's Killer DPPIV= | =Sam's Killer DPPIV= | ||
| - | <StructureSection load='6B1E' size=' | + | <StructureSection load='6B1E' size='450' frame='true' side='right' caption='DPPIV bound to Vildagliptin' scene='10/1037491/Dppiv_beta_propellers/2'> |
| - | + | ||
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==Introduction== | ==Introduction== | ||
=== Function === | === Function === | ||
| + | [https://www.rcsb.org/structure/6B1E DPPIV with Vildagliptin PDB] | ||
=== Inhibitors === | === Inhibitors === | ||
| - | [[Image:DPPIV_Proteopedia_1.png| | + | [[Image:DPPIV_Proteopedia_1.png|300px|Right|thumb|Figure 1. Catalytic triad of DPPIV with Vildagliptin Bound to active site (Catalytic water is shown in Red).]] Vildagliptin Inhibits DPPIV through a covalent bond to the Ser 608 of the catalytic triad.<ref name=”Berger”>PMID:30815539</ref> |
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | + | Structural over view highlighting the catalytic domain <scene name='10/1037491/Catalytic_domain/3'>catalytic domain</scene> | |
| + | Scene representing all the Intxns Vildagliptin shares in the catalytic domain <scene name='10/1037491/Vildagliptin_intxns/2'>Vildaglitpin Binding pocket Intxns</scene> | ||
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| + | Structural over view highlighting/differentiating between the different domains of DPPIV <scene name='10/1037491/Dppiv_domains/1'>DPPIV Domains</scene> | ||
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| + | An Intro movie or just a protein overview <scene name='10/1037491/Dppiv_with_vildagliptin_movie/1'>DPPIV intro movie</scene> | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
| + | <ref name=”Berger”>PMID:30815539</ref> | ||
| + | <ref name=”Ransey”>PMID:28504306</ref> | ||
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<references/> | <references/> | ||
Current revision
Sam's Killer DPPIV
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References
- ↑ Berger JP, SinhaRoy R, Pocai A, Kelly TM, Scapin G, Gao YD, Pryor KAD, Wu JK, Eiermann GJ, Xu SS, Zhang X, Tatosian DA, Weber AE, Thornberry NA, Carr RD. A comparative study of the binding properties, dipeptidyl peptidase-4 (DPP-4) inhibitory activity and glucose-lowering efficacy of the DPP-4 inhibitors alogliptin, linagliptin, saxagliptin, sitagliptin and vildagliptin in mice. Endocrinol Diabetes Metab. 2017 Nov 24;1(1):e00002. doi: 10.1002/edm2.2., eCollection 2018 Jan. PMID:30815539 doi:http://dx.doi.org/10.1002/edm2.2
- ↑ Berger JP, SinhaRoy R, Pocai A, Kelly TM, Scapin G, Gao YD, Pryor KAD, Wu JK, Eiermann GJ, Xu SS, Zhang X, Tatosian DA, Weber AE, Thornberry NA, Carr RD. A comparative study of the binding properties, dipeptidyl peptidase-4 (DPP-4) inhibitory activity and glucose-lowering efficacy of the DPP-4 inhibitors alogliptin, linagliptin, saxagliptin, sitagliptin and vildagliptin in mice. Endocrinol Diabetes Metab. 2017 Nov 24;1(1):e00002. doi: 10.1002/edm2.2., eCollection 2018 Jan. PMID:30815539 doi:http://dx.doi.org/10.1002/edm2.2
- ↑ 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
