3df0

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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains., Moldoveanu T, Gehring K, Green DR, Nature. 2008 Nov 20;456(7220):404-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19020622 19020622]
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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]
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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[[Category: Calpain-2]]
[[Category: Calpain-2]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Gehring, K.]]
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[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
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[[Category: Green, D R.]]
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[[Category: Moldoveanu, T.]]
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[[Category: Alternative splicing]]
[[Category: Alternative splicing]]
[[Category: C2-like domain]]
[[Category: C2-like domain]]
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[[Category: Thiol protease inhibitor]]
[[Category: Thiol protease inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 12 10:47:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 3 20:14:20 2008''

Revision as of 18:14, 3 December 2008

Template:STRUCTURE 3df0

Calcium-dependent complex between m-calpain and calpastatin

Template:ABSTRACT PUBMED 19020622

About this Structure

3DF0 is a 3 chains structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains., Moldoveanu T, Gehring K, Green DR, Nature. 2008 Nov 20;456(7220):404-8. PMID:19020622

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

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

The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium., Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, Irie A, Sorimachi H, Bourenkow G, Bartunik H, Suzuki K, Bode W, Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):588-92. PMID:10639123

A structural model for the inhibition of calpain by calpastatin: crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor., Todd B, Moore D, Deivanayagam CC, Lin GD, Chattopadhyay D, Maki M, Wang KK, Narayana SV, J Mol Biol. 2003 Apr 18;328(1):131-46. PMID:12684003

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[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]

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