Prolyl Endopeptidase: Difference between revisions

No edit summary
Line 8: Line 8:


=== 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 propeller domain is proposed to be very important in allowing the binding of subtrate as well as the inability of PEPs to hydrolyze peptide chains longer than 30 amino acids.
The β-propeller domain is made up of repeated antiparallel β-sheets with connecting peptide strands which form a tight lid over the active site located on the catalytic domain. The β-propeller domain is cylindrical in structure and contains a very tight central channel through its core that is roughly 4Å in diameter in the resting state.


=== Catalytic Domain ===
=== Catalytic Domain ===

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Andrea Gorrell, Stacey Shantz, David Canner, Michal Harel, Alexander Berchansky, Joel L. Sussman