Dipeptidyl peptidase

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Line 44: Line 44:
**[[5ehh]] - hDPP-III (mutant) + endomorphin II<br />
**[[5ehh]] - hDPP-III (mutant) + endomorphin II<br />
**[[3csk]] – DPP-III (mutant) – yeast<br />
**[[3csk]] – DPP-III (mutant) – yeast<br />
 +
**[[5yfb]], [[5yfc]], [[5yfd]] – DPP-III – mushroom<br />
*DPP-IV (CD26)
*DPP-IV (CD26)
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**[[3kwj]], [[3oc0]], [[3kwf]], [[3q8w]] – hDPP-IV extracellular domain +quinoline derivative<br />
**[[3kwj]], [[3oc0]], [[3kwf]], [[3q8w]] – hDPP-IV extracellular domain +quinoline derivative<br />
**[[3g0b]], [[3g0d]], [[3g0g]], [[3nox]], [[3hab]], [[3hac]], [[3f8s]], [[3h0c]], [[3ccb]], [[3ccc]], [[2qjr]], [[2qky]], [[3d4l]], [[2jid]], [[3bjm]], [[2rip]], [[2ole]], [[2rgu]], [[2i78]], [[2oag]], [[2oqv]], [[2oqi]], [[2ogz]], [[2i03]], [[2g5p]], [[2g5t]], [[2g63]], [[2bub]], [[2ajl]], [[1wcy]], [[1rwq]], [[1tkr]], [[1n1m]], [[3eio]], [[3g0c]], [[3opm]], [[3sww]], [[3sx4]], [[3q0t]], [[4a5s]], [[3vjk]], [[3vjl]], [[3vjm]], [[3w2t]], [[4dsa]], [[4dsz]], [[4dtc]], [[4g1f]],[[3o95]], [[3o9v]], [[4j3j]], [[4jh0]], [[4lko]], [[4n8d]], [[4n8e]], [[4pnz]], [[4pv7]], [[3wqh]], [[5i7u]], [[5j3j]], [[5kby]], [[5t4b]], [[5t4e]], [[5t4f]], [[5t4h]] – hDPP-IV extracellular domain+inhibitor<br />
**[[3g0b]], [[3g0d]], [[3g0g]], [[3nox]], [[3hab]], [[3hac]], [[3f8s]], [[3h0c]], [[3ccb]], [[3ccc]], [[2qjr]], [[2qky]], [[3d4l]], [[2jid]], [[3bjm]], [[2rip]], [[2ole]], [[2rgu]], [[2i78]], [[2oag]], [[2oqv]], [[2oqi]], [[2ogz]], [[2i03]], [[2g5p]], [[2g5t]], [[2g63]], [[2bub]], [[2ajl]], [[1wcy]], [[1rwq]], [[1tkr]], [[1n1m]], [[3eio]], [[3g0c]], [[3opm]], [[3sww]], [[3sx4]], [[3q0t]], [[4a5s]], [[3vjk]], [[3vjl]], [[3vjm]], [[3w2t]], [[4dsa]], [[4dsz]], [[4dtc]], [[4g1f]],[[3o95]], [[3o9v]], [[4j3j]], [[4jh0]], [[4lko]], [[4n8d]], [[4n8e]], [[4pnz]], [[4pv7]], [[3wqh]], [[5i7u]], [[5j3j]], [[5kby]], [[5t4b]], [[5t4e]], [[5t4f]], [[5t4h]] – hDPP-IV extracellular domain+inhibitor<br />
 +
**[[6b1e]], [[6b1o]] – hDPP-IV extracellular domain (mutant) +inhibitor<br />
**[[1r9n]], [[2bgr]], [[1nu8]] – hDPP-IV extracellular domain+polypeptide<br />
**[[1r9n]], [[2bgr]], [[1nu8]] – hDPP-IV extracellular domain+polypeptide<br />
**[[1w1i]] – hDPP-IV extracellular domain+adenosine deaminase<br />
**[[1w1i]] – hDPP-IV extracellular domain+adenosine deaminase<br />
Line 62: Line 64:
**[[2aj8]], [[2ajb]], [[2ajc]], [[2ajd]], [[2bua]], [[2buc]], [[1orw]], [[5lls]] – pDPP-IV extracellular domain+inhibitor - pig<br />
**[[2aj8]], [[2ajb]], [[2ajc]], [[2ajd]], [[2bua]], [[2buc]], [[1orw]], [[5lls]] – pDPP-IV extracellular domain+inhibitor - pig<br />
**[[1orv]] - pDPP-IV extracellular domain<br />
**[[1orv]] - pDPP-IV extracellular domain<br />
-
**[[2ecf]] - DPP-IV – ''Stenotrophomonas maltophilia''
+
**[[2ecf]] - DPP-IV – ''Stenotrophomonas maltophilia''<br />
 +
**[[5olj]] – PgDPP-IV – ''Porphyromonas gingivalis''<br />
*DPP-VI
*DPP-VI
**[[3pvq]], [[4r0k]] – DPP-VI – ''Bacterioides thetaiotamicron''
**[[3pvq]], [[4r0k]] – DPP-VI – ''Bacterioides thetaiotamicron''
 +
 +
*DPP-VIII
 +
 +
**[[6eos]], [[6eoo]] – hDPP-VIII <br />
 +
**[[6eot]], [[6eop]] – hDPP-VIII + polypeptide<br />
 +
 +
*DPP-IX
 +
 +
**[[6eoq]], [[6eor]] – hDPP-IX <br />
*DPP-X
*DPP-X
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**[[4wjl]] – hDPP-X extracellular domain<br />
**[[4wjl]] – hDPP-X extracellular domain<br />
-
*DPP-XI or peptidase S46
+
*DPP-XI or peptidase S46 or Asp/Glu-specific DPP
-
**[[4xzy]], [[4y01]], [[4y02]], [[4y04]] – hDPP-XI – ''Porphyromonas gingivalis''<br />
+
**[[4xzy]], [[4y01]], [[4y02]], [[4y04]] – PgDPP-XI <br />
 +
**[[5jxp]], [[5jxk]], [[5jwf]] – PeDPP-XI – ''Porphyromonas endodontalis''<br />
 +
**[[5jy0]], [[5jxf]], [[5jwi]], [[5jwg]] – PeDPP-XI + polypeptide <br />
}}
}}

Revision as of 10:06, 1 May 2018

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

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3D Structures of Dipeptidyl peptidase

Updated on 01-May-2018

References

  1. 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
  2. Pro B, Dang NH. CD26/dipeptidyl peptidase IV and its role in cancer. Histol Histopathol. 2004 Oct;19(4):1345-51. PMID:15375776
  3. 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
  4. 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
  5. 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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