Tripeptidyl peptidase: Difference between revisions
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[[Image:2d5l.png|left|200px|thumb|Crystal Structure of Tripeptidyl peptidase ([[2d5l]])]] | [[Image:2d5l.png|left|200px|thumb|Crystal Structure of Tripeptidyl peptidase ([[2d5l]])]] | ||
{{STRUCTURE_3ee6| PDB=3ee6 | SIZE=400| SCENE= |right|CAPTION=Tripeptidyl peptidase [[3ee6]]}} | {{STRUCTURE_3ee6| PDB=3ee6 | SIZE=400| SCENE= |right|CAPTION=Tripeptidyl peptidase dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, [[3ee6]]}} | ||
[[Tripeptidyl peptidase]] (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides. TPP-I functions in lysosomes, TPP-II is part of the ubiquitin-proteasome pathway. The images at the left and at the right correspond to one representative TPP, ''i.e.'' the crystal structure of Pro-Tripeptidyl peptidase-IV from ''Porphyromonas gingivalis'' ([[2d5l]]). | [[Tripeptidyl peptidase]] (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides. TPP-I functions in lysosomes, TPP-II is part of the ubiquitin-proteasome pathway. The images at the left and at the right correspond to one representative TPP, ''i.e.'' the crystal structure of Pro-Tripeptidyl peptidase-IV from ''Porphyromonas gingivalis'' ([[2d5l]]). | ||
Revision as of 15:22, 18 November 2012
Tripeptidyl peptidase (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides. TPP-I functions in lysosomes, TPP-II is part of the ubiquitin-proteasome pathway. The images at the left and at the right correspond to one representative TPP, i.e. the crystal structure of Pro-Tripeptidyl peptidase-IV from Porphyromonas gingivalis (2d5l).
3D Structures of Tripeptidyl peptidase3D Structures of Tripeptidyl peptidase
TPP-ITPP-I
3ee6 – TPP-I – human
3edy – hTPP-I precursor residues 20-563
TPP-IITPP-II
3lxu – TPP-II residues 463-770 – Drosophila melanogaster
TPP-IVTPP-IV
2eep – PgPro-TPP-IV+inhibitor – Porphyromonas gingivalis
2d5l - PgPro-TPP-IV
2z3w - PgPro-TPP-IV (mutant)
2z3z, 2dcm - PgPro-TPP-IV (mutant)+inhibitor