Dipeptidyl peptidase

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Revision as of 10:42, 24 February 2019

Human glycosylated dipeptidyl peptidase I complex with inhibitor, glycerol and chloride ion (green) (PDB entry 4cdc)

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Updated on 24-February-2019

↑ Sakamoto Y, Suzuki Y, Iizuka I, Tateoka C, Roppongi S, Fujimoto M, Inaka K, Tanaka H, Yamada M, Ohta K, Gouda H, Nonaka T, Ogasawara W, Tanaka N. Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity. Sci Rep. 2015 Jun 9;5:11151. doi: 10.1038/srep11151. PMID:26057589 doi:http://dx.doi.org/10.1038/srep11151
↑ Pro B, Dang NH. CD26/dipeptidyl peptidase IV and its role in cancer. Histol Histopathol. 2004 Oct;19(4):1345-51. PMID:15375776
↑ 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
↑ 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
↑ 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

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 == Structural highlights ==
-Human DPP-I contains 3 chains. <scene name='43/433126/Cv/4'>Light</scene> and <scene name='43/433126/Cv/5'>heavy chains forming the catalytic site</scene> and a <scene name='43/433126/Cv/8'>third chain including the exclusion domain</scene> which is responsible of the exopeptidase activity of DPP-I by partially blocking the active site cleft.  The <scene name='43/433126/Cv/9'>inhibitors binds to a Cys residue at the active site</scene>. <ref>PMID:24592859</ref>
+Human DPP-I contains 3 chains. <scene name='43/433126/Cv/10'>Light</scene> and <scene name='43/433126/Cv/12'>heavy chains forming the catalytic site</scene> and a <scene name='43/433126/Cv/13'>third chain including the exclusion domain</scene> which is responsible of the exopeptidase activity of DPP-I by partially blocking the active site cleft.  The <scene name='43/433126/Cv/14'>inhibitors binds to a Cys residue at the active site</scene>. <ref>PMID:24592859</ref>
 </StructureSection>
 == 3D Structures of Dipeptidyl peptidase ==