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Prolyl Endopeptidase
From Proteopedia
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=== Binding Mechanism === | === Binding Mechanism === | ||
| - | [[Image:1yr2_hing.png]] | + | [[Image:1yr2_hing.png|thumb|alt=Alt text|Peptide chains connecting the catalytic and β-propeller domains]] |
=== Inhibition === | === Inhibition === | ||
Revision as of 18:15, 25 March 2010
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Prolyl endopeptidases (PEPs) are a class of serine proteases which cleave peptide bonds on the c-terminal side of internal proline residues.
Contents |
Structure
β-Propeller Domain
Catalytic Domain
Domain Interface
Function
PEPs are thought to have a role in the degredation of neuropeptides due to the high concentration of PEPs in the brain and the fact that PEPs have been shown to degrade several neuropeptides(vasopressin, β-endorphin, thyroliberin).
Binding Mechanism
Inhibition
Pharmaceutical Possibilities
Celiac Disease
Neurological Disorders
References
Proteopedia Page Contributors and Editors (what is this?)
Stacey Shantz, Michal Harel, Alexander Berchansky, Joel L. Sussman, Andrea Gorrell, David Canner
