1df0

<table><tr><td colspan='2'>[[1df0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DF0 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aj5|1aj5]], [[1alv|1alv]], [[1alw|1alw]], [[1dvi|1dvi]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Calpain-2 Calpain-2], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.53 3.4.22.53] </span></td></tr>

[[https://www.uniprot.org/uniprot/CAN2_RAT CAN2_RAT]] Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. [[https://www.uniprot.org/uniprot/CPNS1_RAT CPNS1_RAT]] Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

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== Publication Abstract from PubMed ==

The combination of thiol protease activity and calmodulin-like EF-hands is a feature unique to the calpains. The regulatory mechanisms governing calpain activity are complex, and the nature of the Ca(2+)-induced switch between inactive and active forms has remained elusive in the absence of structural information. We describe here the 2.6 A crystal structure of m-calpain in the Ca(2+)-free form, which illustrates the structural basis for the inactivity of calpain in the absence of Ca(2+). It also reveals an unusual thiol protease fold, which is associated with Ca(2+)-binding domains through heterodimerization and a C(2)-like beta-sandwich domain. Strikingly, the structure shows that the catalytic triad is not assembled, indicating that Ca(2+)-binding must induce conformational changes that re-orient the protease domains to form a functional active site. The alpha-helical N-terminal anchor of the catalytic subunit does not occupy the active site but inhibits its assembly and regulates Ca(2+)-sensitivity through association with the regulatory subunit. This Ca(2+)-dependent activation mechanism is clearly distinct from those of classical proteases.

Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation.,Hosfield CM, Elce JS, Davies PL, Jia Z EMBO J. 1999 Dec 15;18(24):6880-9. PMID:10601010<ref>PMID:10601010</ref>

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

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== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Calpain-2]]

[[Category: Davies, P L]]

[[Category: Elce, J S]]

[[Category: Hosfield, C M]]

[[Category: Jia, Z]]

[[Category: C2 domain]]

[[Category: Zymogen activation]]