Prolyl Endopeptidase

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	== Function ==		== 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 ===		=== Binding Mechanism ===

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Revision as of 20:02, 24 March 2010

spinqualitylabelsall models Prolyl endopeptidase of Sphingomonas capsulata Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Prolyl endopeptidases (PEPs) are a class of serine proteases which cleave peptide bonds on the c-terminal side of internal proline residues.

Contents 1 Structure 1.1 β-Propeller Domain 1.2 Catalytic Domain 1.3 Domain Interface 2 Function 2.1 Binding Mechanism 2.2 Inhibition 3 Pharmaceutical Possibilities 3.1 Celiac Disease 3.2 Neurological Disorders 4 References

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