6ash: Difference between revisions
Jump to navigation
Jump to search
New page: '''Unreleased structure''' The entry 6ash is ON HOLD until Paper Publication Authors: Law, S., Aguda, A., Nguyen, N., Brayer, G., Bromme, D. Description: Crystal stucture of human Cath... |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure 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 with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6ASH 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]] 1.423Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1XF:2-{[(CARBAMOYLSULFANYL)ACETYL]AMINO}BENZOIC+ACID'>1XF</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=6ash FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ash OCA], [https://pdbe.org/6ash PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ash RCSB], [https://www.ebi.ac.uk/pdbsum/6ash PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ash ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[https://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 == | |||
[https://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. | |||
==See Also== | |||
*[[Cathepsin 3D structures|Cathepsin 3D structures]] | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Law | [[Category: Large Structures]] | ||
[[Category: | [[Category: Aguda A]] | ||
[[Category: Brayer G]] | |||
[[Category: Bromme D]] | |||
[[Category: Law S]] | |||
[[Category: Nguyen N]] | |||
Latest revision as of 17:24, 4 October 2023
Crystal structure of human Cathepsin K with a non-active site inhibitor at 1.42 Angstrom resolutionCrystal structure of human Cathepsin K with a non-active site inhibitor at 1.42 Angstrom resolution
Structural highlights
DiseaseCATK_HUMAN Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:265800. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.[1] [2] [3] [4] FunctionCATK_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. See AlsoReferences
|
| ||||||||||||||||||