Prolyl Endopeptidase: Difference between revisions
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=== β-Propeller Domain === | === β-Propeller Domain === | ||
The β-propeller domain is made up of repeated antiparallel β-sheets forming a tight lid over the active site located on the catalytic domain. This propelleer domain is thought to be very important in the binding of subtrate as well as the inability of PEPs to hydrolyze peptide chains longer than 30 amino acids. | |||
=== Catalytic Domain === | === Catalytic Domain === | ||
=== Domain Interface === | === Domain Interface === | ||