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Revision as of 13:35, 26 March 2024

DPPIV in Humans

spinqualitylabelsall models PDB 6B1E for DPPIV in complex with Vildagliptin Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Introduction 1.1 History 1.2 Function 2 Structure 2.1 Overview 2.2 Catalytic Triad 2.3 Mechanism 2.4 Inhibitors 3 Relevance 3.1 Diabetes 3.2 HIV/AIDS Introduction Image of DPPIV Proline Peptidase Overview History discovery and whatnot Function town tartness Structure [1] Overview Catalytic Triad [1] Mechanism The picture of the mechanism is inserted but not visible, maybe too high of a quality? Error creating thumbnail: libgomp: Thread creation failed: Resource temporarily unavailable Figure 5. Mechanism of the catalytic triad of DPPIV. Inhibitors Relevance Diabetes HIV/AIDS

References

1. ↑ ^{1.0 1.1} Hiramatsu H, Kyono K, Higashiyama Y, Fukushima C, Shima H, Sugiyama S, Inaka K, Yamamoto A, Shimizu R. The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold. Biochem Biophys Res Commun. 2003 Mar 21;302(4):849-54. PMID:12646248

Student Contributors

• Karisma Moll
• Merritt Jugo
• Sam Magnabosco