Prolyl Endopeptidase: Difference between revisions
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<applet load='1yr2' size='300' frame='true' align='right' caption='Prolyl endopeptidase of Sphingomonas capsulata at 1.80Å' /> | <applet load='1yr2' size='300' frame='true' align='right' caption='Prolyl endopeptidase of Sphingomonas capsulata at 1.80Å' /> | ||
Prolyl endopeptidases (PEPs) are a class of serine proteases which cleave peptide bonds on the | Prolyl endopeptidases (PEPs) are a class of serine proteases which cleave peptide bonds on the C-terminal side of internal proline residues. | ||
== Structure == | == Structure == | ||
[[Image:1yr2_ribbon2.png|thumb|alt=Alt text|Catalytic( and β-propeller domains(]] | |||
Prolyl endopeptidases are relatively large enzymes(75 kDa) and contain two distinct domains: a catalytic domain and a β-propeller domain. | |||
=== β-Propeller Domain === | === β-Propeller Domain === | ||
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=== Binding Mechanism === | === Binding Mechanism === | ||
=== Inhibition === | === Inhibition === | ||