3df0
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 3DF0 is a | + | 3DF0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DF0 OCA]. |
==Reference== | ==Reference== | ||
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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] | ||
[[Category: Calpain-2]] | [[Category: Calpain-2]] | ||
| + | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Pdbx_ordinal=, <PDBx:audit_author.]] | [[Category: Pdbx_ordinal=, <PDBx:audit_author.]] | ||
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[[Category: Thiol protease inhibitor]] | [[Category: Thiol protease inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 3 20: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 3 20:37:44 2008'' |
Revision as of 03:45, 4 December 2008
Calcium-dependent complex between m-calpain and calpastatin
Template:ABSTRACT PUBMED 19020622
About this Structure
3DF0 is a Protein complex 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.]]
Page seeded by OCA on Wed Dec 3 20:37:44 2008
Categories: Calpain-2 | Protein complex | Rattus norvegicus | Alternative splicing | C2-like domain | Calcium | Cytoplasm | Hydrolase | Inhibitor loop-out | Membrane | Penta ef-hand domain | Phosphoprotein | Protease | Protease core domain | Protease inhibitor | Thiol protease | Thiol protease inhibitor
