1tl9

<table><tr><td colspan='2'>[[1tl9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TL9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TL9 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AR7:AMINO{[(4S)-4-AMINO-5,5-DIHYDROXYPENTYL]AMINO}METHANIMINIUM'>AR7</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;'>[[1kxr|1kxr]], [[1mdw|1mdw]], [[1dfo|1dfo]], [[1kfu|1kfu]], [[1kfx|1kfx]], [[1nx0|1nx0]], [[1tlo|1tlo]]</div></td></tr>

<tr id='gene'><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 Buffalo rat])</td></tr>

<tr id='activity'><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>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tl9 OCA], [http://pdbe.org/1tl9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tl9 RCSB], [http://www.ebi.ac.uk/pdbsum/1tl9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tl9 ProSAT]</span></td></tr>

[[http://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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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1tl9" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Calpain-1]]

[[Category: Campbell, R L]]

[[Category: Cuerrier, D]]

[[Category: Davies, P L]]

[[Category: Moldoveanu, T]]

[[Category: Covalently-linked inhibitor at the active site cysteine forms a hemithioacetal]]

[[Category: Hydrolase]]

[[Category: Hydrolase-hydrolase inhibitor complex]]