Prolyl Endopeptidase
From Proteopedia
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<applet load='1yr2' size='300' frame='true' align='right' caption='Prolyl endopeptidase of Sphingomonas capsulata' /> | <applet load='1yr2' size='300' frame='true' align='right' caption='Prolyl endopeptidase of Sphingomonas capsulata' /> | ||
| - | Prolyl endopeptidases (PEPs) are a class of serine proteases which cleave peptide bonds on the c-terminal side of internal proline residues. | + | 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. |
== Structure == | == Structure == | ||
Revision as of 19:55, 24 March 2010
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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 |
Structure
β-Propeller Domain
Catalytic Domain
Domain Interface
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
