5i4h: Difference between revisions
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The | ==Caught in the Act: The Crystal Structure of cleaved Cathepsin L bound to the active site of Cathepsin L== | ||
<StructureSection load='5i4h' size='340' side='right' caption='[[5i4h]], [[Resolution|resolution]] 1.42Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5i4h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I4H FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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_L Cathepsin L], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.15 3.4.22.15] </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=5i4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i4h OCA], [http://pdbe.org/5i4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i4h RCSB], [http://www.ebi.ac.uk/pdbsum/5i4h PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CATL1_HUMAN CATL1_HUMAN]] Important for the overall degradation of proteins in lysosomes. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cathepsin L is a ubiquitously expressed papain-like cysteine protease involved in the endosomal degradation of proteins and has numerous roles in physiological and pathological processes, such as arthritis, osteoporosis, and cancer. Insight into the specificity of cathepsin L is important for elucidating its physiological roles and drug discovery. To study interactions with synthetic ligands, we prepared a presumably inactive mutant and crystallized it. Unexpectedly, the crystal structure determined at 1.4 A revealed that the cathepsin L molecule is cleaved, with the cleaved region trapped in the active site cleft of the neighboring molecule. Hence, the catalytic mutant demonstrated low levels of catalytic activity. | |||
Caught in the act: the crystal structure of cleaved cathepsin L bound to the active site of Cathepsin L.,Sosnowski P, Turk D FEBS Lett. 2016 Apr;590(8):1253-61. doi: 10.1002/1873-3468.12140. Epub 2016 Mar, 30. PMID:26992470<ref>PMID:26992470</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5i4h" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cathepsin L]] | |||
[[Category: Sosnowski, P]] | [[Category: Sosnowski, P]] | ||
[[Category: Turk, D]] | [[Category: Turk, D]] | ||
[[Category: Cathepsin]] | |||
[[Category: Cysteine cathepsin]] | |||
[[Category: Hydrolase]] | |||
[[Category: Interaction]] | |||
[[Category: Substrate]] | |||
