4ktu

Bovine trypsin in complex with microviridin J at pH 6.5

spinqualitylabelsall models 4ktu, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ktu is a 2 chain structure with sequence from Bos taurus and Microcystis aeruginosa MRC. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Ligands: ACE, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRY1_BOVIN Publication Abstract from PubMed Understanding and controlling proteolysis is an important goal in therapeutic chemistry. Among the natural products specifically inhibiting proteases microviridins are particularly noteworthy. Microviridins are ribosomally produced and posttranslationally modified peptides that are processed into a unique, cagelike architecture. Here, we report a combined rational and random mutagenesis approach that provides fundamental insights into selectivity-conferring moieties of microviridins. The potent variant microviridin J was co-crystallized with trypsin, and for the first time the three-dimensional structure of microviridins was determined and the mode of inhibition revealed. Harnessing the evolvability of tricyclic microviridins to dissect protease-inhibitor interactions.,Weiz AR, Ishida K, Quitterer F, Meyer S, Kehr JC, Muller KM, Groll M, Hertweck C, Dittmann E Angew Chem Int Ed Engl. 2014 Apr 1;53(14):3735-8. doi: 10.1002/anie.201309721., Epub 2014 Mar 3. PMID:24591244 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin 3D structures

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