6ash
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal stucture of human Cathepsin K with a non-active site inhibitor at 1.42 Angstrom resolution== | |
| - | + | <StructureSection load='6ash' size='340' side='right' caption='[[6ash]], [[Resolution|resolution]] 1.42Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6ash]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ASH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ASH FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1XF:2-{[(CARBAMOYLSULFANYL)ACETYL]AMINO}BENZOIC+ACID'>1XF</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_K Cathepsin K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.38 3.4.22.38] </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=6ash FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ash OCA], [http://pdbe.org/6ash PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ash RCSB], [http://www.ebi.ac.uk/pdbsum/6ash PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ash ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[http://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref> <ref>PMID:9529353</ref> <ref>PMID:10491211</ref> <ref>PMID:10878663</ref> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cathepsin K]] | ||
| + | [[Category: Aguda, A]] | ||
[[Category: Brayer, G]] | [[Category: Brayer, G]] | ||
[[Category: Bromme, D]] | [[Category: Bromme, D]] | ||
| + | [[Category: Law, S]] | ||
[[Category: Nguyen, N]] | [[Category: Nguyen, N]] | ||
| - | [[Category: | + | [[Category: Cathepsin k]] |
| - | [[Category: | + | [[Category: Exosite]] |
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Hydrolase- hydrolase inhibitor complex]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
| + | [[Category: Inhibitor]] | ||
Revision as of 07:24, 29 August 2018
Crystal stucture of human Cathepsin K with a non-active site inhibitor at 1.42 Angstrom resolution
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