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3iv2
From Proteopedia
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| - | [[Image:3iv2.png|left|200px]] | ||
| - | + | ==Crystal structure of mature apo-Cathepsin L C25A mutant== | |
| + | <StructureSection load='3iv2' size='340' side='right'caption='[[3iv2]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3iv2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IV2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IV2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3k24|3k24]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTSL1, CTSL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cathepsin_L Cathepsin L], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3iv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iv2 OCA], [https://pdbe.org/3iv2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iv2 RCSB], [https://www.ebi.ac.uk/pdbsum/3iv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iv2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/CATL1_HUMAN CATL1_HUMAN]] Important for the overall degradation of proteins in lysosomes. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iv/3iv2_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3iv2 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Proteolysis of eukaryotic histone tails has emerged as an important factor in the modulation of cell-cycle progression and cellular differentiation. The recruitment of lysosomal cathepsin L to the nucleus where it mediates proteolysis of the mouse histone H3 tail has been described recently. Here, we report the three-dimensional crystal structures of a mature, inactive mutant of human cathepsin L alone and in complex with a peptide derived from histone H3. Canonical substrate-cathepsin L interactions are observed in the complex between the protease and the histone H3 peptide. Systematic analysis of the impact of posttranslational modifications at histone H3 on substrate selectivity suggests cathepsin L to be highly accommodating of all modified peptides. This is the first report of cathepsin L-histone H3 interaction and the first structural description of cathepsin L in complex with a substrate. | ||
| - | + | Structural basis for the recognition and cleavage of histone H3 by cathepsin L.,Adams-Cioaba MA, Krupa JC, Xu C, Mort JS, Min J Nat Commun. 2011 Feb;2:197. PMID:21326229<ref>PMID:21326229</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3iv2" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Cathepsin|Cathepsin]] | + | *[[Cathepsin 3D structures|Cathepsin 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Cathepsin L]] | [[Category: Cathepsin L]] | ||
| - | [[Category: | + | [[Category: Human]] |
| - | [[Category: Adams-Cioaba, M A | + | [[Category: Large Structures]] |
| - | [[Category: Arrowsmith, C H | + | [[Category: Adams-Cioaba, M A]] |
| - | [[Category: Bochkarev, A | + | [[Category: Arrowsmith, C H]] |
| - | [[Category: Bountra, C | + | [[Category: Bochkarev, A]] |
| - | [[Category: Edwards, A M | + | [[Category: Bountra, C]] |
| - | [[Category: Krupa, J C | + | [[Category: Edwards, A M]] |
| - | [[Category: Min, J | + | [[Category: Krupa, J C]] |
| - | [[Category: Mort, J S | + | [[Category: Min, J]] |
| - | [[Category: Weigelt, J | + | [[Category: Mort, J S]] |
| + | [[Category: Weigelt, J]] | ||
[[Category: Apo]] | [[Category: Apo]] | ||
[[Category: Disulfide bond]] | [[Category: Disulfide bond]] | ||
Current revision
Crystal structure of mature apo-Cathepsin L C25A mutant
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Categories: Cathepsin L | Human | Large Structures | Adams-Cioaba, M A | Arrowsmith, C H | Bochkarev, A | Bountra, C | Edwards, A M | Krupa, J C | Min, J | Mort, J S | Weigelt, J | Apo | Disulfide bond | Glycoprotein | Hydrolase | Lysosome | Mutant | Protease | Thiol protease | Zymogen

