This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3k24

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 3k24 is ON HOLD Authors: Adams-Cioaba, M.A., Krupa, J.C., Mort, J.S., Min, J., Structural Genomics Consortium (SGC) Description: Crystal structure ...)
Current revision (08:07, 6 September 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 3k24 is ON HOLD
+
==Crystal structure of mature apo-Cathepsin L C25A mutant in complex with Gln-Leu-Ala peptide==
 +
<StructureSection load='3k24' size='340' side='right'caption='[[3k24]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3k24]] is a 4 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=3K24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K24 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]] 2.5&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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=3k24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k24 OCA], [https://pdbe.org/3k24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k24 RCSB], [https://www.ebi.ac.uk/pdbsum/3k24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k24 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/k2/3k24_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=3k24 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.
-
Authors: Adams-Cioaba, M.A., Krupa, J.C., Mort, J.S., Min, J., Structural Genomics Consortium (SGC)
+
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>
-
Description: Crystal structure of a human protease in complex with a peptide substrate
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3k24" style="background-color:#fffaf0;"></div>
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 7 13:45:13 2009''
+
==See Also==
 +
*[[Cathepsin 3D structures|Cathepsin 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Adams-Cioaba MA]]
 +
[[Category: Arrowsmith CH]]
 +
[[Category: Bochkarev A]]
 +
[[Category: Bountra C]]
 +
[[Category: Edwards AM]]
 +
[[Category: Krupa JC]]
 +
[[Category: Min J]]
 +
[[Category: Mort JS]]
 +
[[Category: Weigelt J]]

Current revision

Crystal structure of mature apo-Cathepsin L C25A mutant in complex with Gln-Leu-Ala peptide

PDB ID 3k24

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3k24"
Personal tools