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- W1967791344 abstract "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." @default.
- W1967791344 created "2016-06-24" @default.
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- W1967791344 date "2004-11-01" @default.
- W1967791344 modified "2023-10-14" @default.
- W1967791344 title "Crystal Structures of Calpain–E64 and –Leupeptin Inhibitor Complexes Reveal Mobile Loops Gating the Active Site" @default.
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- W1967791344 doi "https://doi.org/10.1016/j.jmb.2004.09.016" @default.
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