This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Prolyl Endopeptidase
From Proteopedia
(Difference between revisions)
| Line 5: | Line 5: | ||
== Structure == | == Structure == | ||
| + | === β-Propeller Domain === | ||
| - | + | === Catalytic Domain === | |
Revision as of 19:39, 24 March 2010
|
Prolyl endopeptidases (PEPs) are a class of serine proteases known to have a role in the degradation of neuropeptides and peptide hormones. PEPs are large enzymes (75kDa) that cleave after proline residues in the peptide chain.
Contents |
Structure
β-Propeller Domain
Catalytic Domain
Function
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
