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1tlo

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[[Image:1tlo.png|left|200px]]
 
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==High resolution crystal structure of calpain I protease core in complex with E64==
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The line below this paragraph, containing "STRUCTURE_1tlo", creates the "Structure Box" on the page.
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<StructureSection load='1tlo' size='340' side='right'caption='[[1tlo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1tlo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TLO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene></td></tr>
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{{STRUCTURE_1tlo| PDB=1tlo | SCENE= }}
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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=1tlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tlo OCA], [https://pdbe.org/1tlo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tlo RCSB], [https://www.ebi.ac.uk/pdbsum/1tlo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tlo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAN1_RAT CAN1_RAT] Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
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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/tl/1tlo_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=1tlo 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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The endogenous calpain inhibitor, calpastatin, modulates some patho-physiological aspects of calpain signaling. Excess calpain can escape this inhibition and as well, many calpain isoforms and autolytically generated protease core fragments are not inhibited by calpastatin. There is a need, therefore, to develop specific, cell-permeable calpain inhibitors to block uncontrolled proteolysis and prevent tissue damage during brain and heart ischemia, spinal-cord injury and Alzheimer's diseases. Here, we report the first high-resolution crystal structures of rat mu-calpain protease core complexed with two traditional, low molecular mass inhibitors, leupeptin and E64. These structures show that access to a slightly deeper, but otherwise papain-like active site is gated by two flexible loops. These loops are divergent among the calpain isoforms giving a potential structural basis for substrate/inhibitor selectivity over other papain-like cysteine proteases and between members of the calpain family.
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===High resolution crystal structure of calpain I protease core in complex with E64===
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Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site.,Moldoveanu T, Campbell RL, Cuerrier D, Davies PL J Mol Biol. 2004 Nov 5;343(5):1313-26. PMID:15491615<ref>PMID:15491615</ref>
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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 1tlo" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15491615}}, adds the Publication Abstract to the page
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*[[Calpain 3D structures|Calpain 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15491615 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15491615}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[1tlo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLO OCA].
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==Reference==
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<ref group="xtra">PMID:15491615</ref><ref group="xtra">PMID:12665854</ref><references group="xtra"/>
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[[Category: Calpain-1]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Campbell, R L.]]
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[[Category: Campbell RL]]
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[[Category: Cuerrier, D.]]
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[[Category: Cuerrier D]]
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[[Category: Davies, P L.]]
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[[Category: Davies PL]]
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[[Category: Moldoveanu, T.]]
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[[Category: Moldoveanu T]]
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[[Category: Hydrolase]]
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Current revision

High resolution crystal structure of calpain I protease core in complex with E64

PDB ID 1tlo

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