4bsq: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 4bsq is ON HOLD  until Paper Publication
+==MOUSE CATHEPSIN S WITH COVALENT LIGAND==
+<StructureSection load='4bsq' size='340' side='right'caption='[[4bsq]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4bsq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BSQ 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]] 1.96&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=QQV:(1R,2R,4R)-N-(2-AZANYLIDENEETHYL)-2-MORPHOLIN-4-YLCARBONYL-4-(PHENYLSULFONYL)CYCLOPENTANE-1-CARBOXAMIDE'>QQV</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4bsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bsq OCA], [https://pdbe.org/4bsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bsq RCSB], [https://www.ebi.ac.uk/pdbsum/4bsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bsq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CATS_MOUSE CATS_MOUSE] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Starting from the weakly active dual CatS/K inhibitor 5, structure-based design supported by X-ray analysis led to the discovery of the potent and selective (&gt;50 000-fold vs CatK) cyclopentane derivative 22 by exploiting specific ligand-receptor interactions in the S2 pocket of CatS. Changing the central cyclopentane scaffold to the analogous pyrrolidine derivative 57 decreased the enzyme as well as the cell-based activity significantly by 24- and 69-fold, respectively. The most promising scaffold identified was the readily accessible proline derivative (e.g., 79). This compound, with an appealing ligand efficiency (LE) of 0.47, included additional structural modifications binding in the S1 and S3 pockets of CatS, leading to favorable in vitro and in vivo properties. Compound 79 reduced IL-2 production in a transgenic DO10.11 mouse model of antigen presentation in a dose-dependent manner with an ED50 of 5 mg/kg.
-Authors: Banner, D.W., Benz, J., Gsell, B., Stihle, M., Ruf, A., Hilpert, H.
+Identification of Potent and Selective Cathepsin S Inhibitors Containing Different Central Cyclic Scaffolds.,Hilpert H, Mauser H, Humm R, Anselm L, Kuehne H, Hartmann G, Gruener S, Banner DW, Benz J, Gsell B, Kuglstatter A, Stihle M, Thoma R, Sanchez RA, Iding H, Wirz B, Haap W J Med Chem. 2013 Nov 22. PMID:24224654<ref>PMID:24224654</ref>
-Description: MOUSE CATHEPSIN S WITH COVALENT LIGAND
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4bsq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cathepsin 3D structures|Cathepsin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Banner DW]]
+[[Category: Benz J]]
+[[Category: Gsell B]]
+[[Category: Hilpert H]]
+[[Category: Ruf A]]
+[[Category: Stihle M]]