Dipeptidyl peptidase

From Proteopedia

Revision as of 13:30, 30 December 2015

spinqualitylabelsall models Human glycosylated dipeptidyl peptidase I complex with inhibitor, glycerol and chloride ion (green) (PDB entry 4cdc) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Disease 4 Structural highlights Function Dipeptidyl peptidase (DPP) is an enzyme which cleaves dipeptides from polypeptides. DPP-I or cathepsin C is involved in inflammatory diseases. DPP-II is a serine protease. DPP-III acts similarly to DPP-IV. DPP-IV (or CD26) cleaves proline dipeptides from the N-termini and is associated with immune regulation. For details see: Dipeptidyl peptidase IV and Dipeptidyl Peptidase-4 Inhibitor Pharmacokinetics. Relevance DPP-IV level is alternating in certain malignancies.[1] DPP-IV inhibitors control body glucose levels and provide potential advantages in diabetes type 2 therapies.[2] Disease DPP-IV is involved in the development of various chronic liver disease like hepatitis C virus infection.[3] Structural highlights Human DPP-I contains 3 chains. Light and heavy chains forming the catalytic site and a third chain including the exclusion domain which is responsible of the exopeptidase activity of DPP-I by partially blocking the active site cleft. The inhibitors binds to a Cys residue at the active site. [4]

3D Structures of Dipeptidyl peptidase

Updated on 30-December-2015

References

1. ↑ Pro B, Dang NH. CD26/dipeptidyl peptidase IV and its role in cancer. Histol Histopathol. 2004 Oct;19(4):1345-51. PMID:15375776
2. ↑ Barnett A. DPP-4 inhibitors and their potential role in the management of type 2 diabetes. Int J Clin Pract. 2006 Nov;60(11):1454-70. PMID:17073841 doi:10.1111/j.1742-1241.2006.01178.x
3. ↑ Itou M, Kawaguchi T, Taniguchi E, Sata M. Dipeptidyl peptidase-4: a key player in chronic liver disease. World J Gastroenterol. 2013 Apr 21;19(15):2298-306. doi:, 10.3748/wjg.v19.i15.2298. PMID:23613622 doi:http://dx.doi.org/10.3748/wjg.v19.i15.2298
4. ↑ Furber M, Tiden AK, Gardiner P, Mete A, Ford R, Millichip I, Stein L, Mather A, Kinchin E, Luckhurst C, Barber S, Cage P, Sanganee H, Austin R, Chohan K, Beri R, Thong B, Wallace A, Oreffo V, Hutchinson R, Harper S, Debreczeni J, Breed J, Wissler L, Edman K. Cathepsin C Inhibitors: Property Optimization and Identification of a Clinical Candidate. J Med Chem. 2014 Mar 14. PMID:24592859 doi:http://dx.doi.org/10.1021/jm401705g