Prolyl Endopeptidase

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	== Structure ==		== Structure ==
		+	=== β-Propeller Domain ===
-		+	=== Catalytic Domain ===

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Revision as of 19:39, 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 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 1 Structure 1.1 β-Propeller Domain 1.2 Catalytic Domain 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

Function

Binding Mechanism

Inhibition

Pharmaceutical Possibilities

Celiac Disease

Neurological Disorders

References