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1tl9

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{{STRUCTURE_1tl9| PDB=1tl9 | SCENE= }}
{{STRUCTURE_1tl9| PDB=1tl9 | SCENE= }}
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'''High resolution crystal structure of calpain I protease core in complex with leupeptin'''
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===High resolution crystal structure of calpain I protease core in complex with leupeptin===
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==Overview==
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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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The line below this paragraph, {{ABSTRACT_PUBMED_15491615}}, adds the Publication Abstract to the page
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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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{{ABSTRACT_PUBMED_15491615}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15491615 15491615]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15491615 15491615]
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A Ca(2+) switch aligns the active site of calpain., Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL, Cell. 2002 Mar 8;108(5):649-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11893336 11893336]
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Calpain silencing by a reversible intrinsic mechanism., Moldoveanu T, Hosfield CM, Lim D, Jia Z, Davies PL, Nat Struct Biol. 2003 May;10(5):371-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12665854 12665854]
[[Category: Calpain-1]]
[[Category: Calpain-1]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Moldoveanu, T.]]
[[Category: Moldoveanu, T.]]
[[Category: Covalently-linked inhibitor at the active site cysteine forms a hemithioacetal]]
[[Category: Covalently-linked inhibitor at the active site cysteine forms a hemithioacetal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:05:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:12:33 2008''

Revision as of 18:12, 28 July 2008

Image:1tl9.png

Template:STRUCTURE 1tl9

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

Template:ABSTRACT PUBMED 15491615

About this Structure

1TL9 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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

A Ca(2+) switch aligns the active site of calpain., Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL, Cell. 2002 Mar 8;108(5):649-60. PMID:11893336

Calpain silencing by a reversible intrinsic mechanism., Moldoveanu T, Hosfield CM, Lim D, Jia Z, Davies PL, Nat Struct Biol. 2003 May;10(5):371-8. PMID:12665854

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