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3iv2

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(New page: '''Unreleased structure''' The entry 3iv2 is ON HOLD Authors: Adams-Cioaba, M.A., Krupa, J.C., Mort, J.S., Min, J. Description: Crystal structure of a human protease C25A mutant, apo f...)
Current revision (12:15, 13 October 2021) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3iv2 is ON HOLD
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==Crystal structure of mature apo-Cathepsin L C25A mutant==
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<StructureSection load='3iv2' size='340' side='right'caption='[[3iv2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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<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>
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<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>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/CATL1_HUMAN CATL1_HUMAN]] Important for the overall degradation of proteins in lysosomes.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iv/3iv2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Adams-Cioaba, M.A., Krupa, J.C., Mort, J.S., Min, J.
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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>
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Description: Crystal structure of a human protease C25A mutant, apo form
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3iv2" style="background-color:#fffaf0;"></div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 9 09:08:10 2009''
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==See Also==
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*[[Cathepsin 3D structures|Cathepsin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Cathepsin L]]
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[[Category: Human]]
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[[Category: Large Structures]]
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[[Category: Adams-Cioaba, M A]]
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[[Category: Arrowsmith, C H]]
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[[Category: Bochkarev, A]]
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[[Category: Bountra, C]]
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[[Category: Edwards, A M]]
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[[Category: Krupa, J C]]
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[[Category: Min, J]]
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[[Category: Mort, J S]]
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[[Category: Weigelt, J]]
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[[Category: Apo]]
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[[Category: Disulfide bond]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Lysosome]]
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[[Category: Mutant]]
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[[Category: Protease]]
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[[Category: Thiol protease]]
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[[Category: Zymogen]]

Current revision

Crystal structure of mature apo-Cathepsin L C25A mutant

PDB ID 3iv2

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