Prolyl Endopeptidase

From Proteopedia

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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. Proline residues are often stable to proteases due to their unique structure and even PEPs require a trans peptide bond preceeding proline for hydrolysis to occur.

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

Binding Mechanism

Inhibition

Pharmaceutical Possibilities

Celiac Disease

Neurological Disorders

References