4Q2K: Bovine Alpha Chymotrypsin Bound To A Cyclic Peptide Inhibitor, 5b

There is a real need for simple structures that define a beta-strand conformation, a secondary structure that is central to peptide-protein interactions. For example, protease substrates and inhibitors almost universally adopt this geometry on active site binding. A planar pyrrole is used to replace two amino acids of a peptide backbone to generate a simple macrocycle that retains the required geometry for active site binding. The resulting beta-strand templates have reduced peptide character and provide potent protease inhibitors with the attachment of an appropriate amino aldehyde to the C-terminus. Picomolar inhibitors of cathepsin L and S are reported and the mode of binding of one example to the model protease chymotrypsin is defined by X-ray crystallography.
PDB ID: 4Q2KDownload
MMDB ID: 121755
PDB Deposition Date: 2014/4/9
Updated in MMDB: 2014/07
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 4Q2K: dimeric; determined by author
Molecular Components in 4Q2K
Label Count Molecule
Proteins (2 molecules)
Chymotrypsinogen a(Gene symbol: CTRB2)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB