Prolyl Endopeptidase

From Proteopedia

Revision as of 18:15, 25 March 2010 by Stacey Shantz (Talk | contribs)
Jump to: navigation, search

Prolyl endopeptidase of Sphingomonas capsulata at 1.80Å

Drag the structure with the mouse to rotate

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

Image:1yr2 hing.png
Peptide chains connecting the catalytic and β-propeller domains

Inhibition

Pharmaceutical Possibilities

Celiac Disease

Neurological Disorders

References

Personal tools