4kts
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Bovine trypsin in complex with microviridin J at pH 8.5== | |
| + | <StructureSection load='4kts' size='340' side='right'caption='[[4kts]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4kts]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Microcystis_aeruginosa_MRC Microcystis aeruginosa MRC]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KTS FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kts OCA], [https://pdbe.org/4kts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kts RCSB], [https://www.ebi.ac.uk/pdbsum/4kts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kts ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24591244</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4kts" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Trypsin 3D structures|Trypsin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Microcystis aeruginosa MRC]] | ||
| + | [[Category: Dittmann E]] | ||
| + | [[Category: Groll M]] | ||
| + | [[Category: Hertweck C]] | ||
| + | [[Category: Quitterer F]] | ||
Current revision
Bovine trypsin in complex with microviridin J at pH 8.5
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