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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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<StructureSection load='1tlo' size='340' side='right' caption='[[1tlo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TLO FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kxr|1kxr]], [[1mdw|1mdw]], [[1dfo|1dfo]], [[1kfu|1kfu]], [[1kfx|1kfx]], [[1nx0|1nx0]], [[1tl9|1tl9]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAPN1, CLS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calpain-1 Calpain-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 3.4.22.52] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tlo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tlo RCSB], [http://www.ebi.ac.uk/pdbsum/1tlo PDBsum]</span></td></tr>
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<table>
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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/chain_selection.php?pdb_ID=2ata 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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{{STRUCTURE_1tlo| PDB=1tlo | SCENE= }}
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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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===High resolution crystal structure of calpain I protease core in complex with E64===
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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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{{ABSTRACT_PUBMED_15491615}}
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==About this Structure==
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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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==See Also==
==See Also==
*[[Calpain|Calpain]]
*[[Calpain|Calpain]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015491615</ref><ref group="xtra">PMID:012665854</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Calpain-1]]
[[Category: Calpain-1]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]

Revision as of 21:09, 28 September 2014

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

1tlo, resolution 1.90Å

Drag the structure with the mouse to rotate

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