Prolyl Endopeptidase
From Proteopedia
(Difference between revisions)
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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 | + | Prolyl endopeptidases (PEPs) are a class of serine proteases which cleave peptide bonds on the c-terminal side of internal proline residues. |
== Structure == | == Structure == | ||
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=== Catalytic Domain === | === Catalytic Domain === | ||
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| + | === Domain Interface === | ||
Revision as of 19:51, 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.
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
