5qbv: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "5qbv" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of human Cathepsin-S with bound ligand== | |||
<StructureSection load='5qbv' size='340' side='right' caption='[[5qbv]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5qbv]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mpf 3mpf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5QBV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5QBV FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=N2D:N-[2-CHLORO-5-(1-{3-[4-(6-CHLORO-3-METHYL-2-OXO-2,3-DIHYDRO-1H-BENZIMIDAZOL-1-YL)PIPERIDIN-1-YL]PROPYL}-6-OXO-1,6-DIHYDROPYRIDAZIN-3-YL)BENZYL]BENZAMIDE'>N2D</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5qbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qbv OCA], [http://pdbe.org/5qbv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5qbv RCSB], [http://www.ebi.ac.uk/pdbsum/5qbv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5qbv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN]] 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 == | |||
A pyridazin-4-one fragment 4 (hCatS IC(50)=170 microM) discovered through Tethering was modeled into cathepsin S and predicted to overlap in S2 with the tetrahydropyridinepyrazole core of a previously disclosed series of CatS inhibitors. This fragment served as a template to design pyridazin-3-one 12 (hCatS IC(50)=430 nM), which also incorporates P3 and P5 binding elements. A crystal structure of 12 bound to Cys25Ser CatS led to the synthesis of the potent diazinone isomers 22 (hCatS IC(50)=60 nM) and 27 (hCatS IC(50)=40 nM). | |||
Diazinones as P2 replacements for pyrazole-based cathepsin S inhibitors.,Ameriks MK, Bembenek SD, Burdett MT, Choong IC, Edwards JP, Gebauer D, Gu Y, Karlsson L, Purkey HE, Staker BL, Sun S, Thurmond RL, Zhu J Bioorg Med Chem Lett. 2010 Jul 15;20(14):4060-4. Epub 2010 May 25. PMID:20541404<ref>PMID:20541404</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Burley, S]] | <div class="pdbe-citations 5qbv" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cathepsin S]] | |||
[[Category: Ameriks, M K]] | |||
[[Category: Bembenek, S D]] | |||
[[Category: Burley, S K]] | |||
[[Category: Mirzadegan, T]] | |||
[[Category: Shao, C]] | |||
[[Category: Yang, H]] | [[Category: Yang, H]] | ||
[[Category: | [[Category: Cathepsin s]] | ||
[[Category: D3r]] | |||
[[Category: Hydrolase]] | |||
[[Category: Ligand docking]] | |||
Revision as of 06:01, 20 December 2017
Crystal structure of human Cathepsin-S with bound ligand
| ||||||||||||
