4q2k

Bovine alpha chymotrypsin bound to a cyclic peptide inhibitor, 5bBovine alpha chymotrypsin bound to a cyclic peptide inhibitor, 5b

Structural highlights 4q2k is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CTRA_BOVIN Publication Abstract from PubMed 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. Macrocyclic protease inhibitors with reduced Peptide character.,Chua KC, Pietsch M, Zhang X, Hautmann S, Chan HY, Bruning JB, Gutschow M, Abell AD Angew Chem Int Ed Engl. 2014 Jul 21;53(30):7828-31. doi: 10.1002/anie.201404301. , Epub 2014 Jun 5. PMID:24903745 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chymotrypsin 3D structures

spinqualitylabelsall models 4q2k, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image