Tripeptidyl peptidase

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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 dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, [[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]]}}
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Revision as of 12:22, 18 November 2012

Image:2d5l.png
Crystal Structure of Tripeptidyl peptidase (2d5l)

Template:STRUCTURE 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).

Contents

3D Structures of Tripeptidyl peptidase

TPP-I

3ee6 – TPP-I – human
3edy – hTPP-I precursor residues 20-563

TPP-II

3lxu – TPP-II residues 463-770 – Drosophila melanogaster

TPP-IV

2eep – PgPro-TPP-IV+inhibitor – Porphyromonas gingivalis
2d5l - PgPro-TPP-IV
2z3w - PgPro-TPP-IV (mutant)
2z3z, 2dcm - PgPro-TPP-IV (mutant)+inhibitor

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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