3df0: Difference between revisions
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[[Image:3df0.png|left|200px]] | [[Image:3df0.png|left|200px]] | ||
{{STRUCTURE_3df0| PDB=3df0 | SCENE= }} | {{STRUCTURE_3df0| PDB=3df0 | SCENE= }} | ||
===Calcium-dependent complex between m-calpain and calpastatin=== | ===Calcium-dependent complex between m-calpain and calpastatin=== | ||
{{ABSTRACT_PUBMED_19020622}} | {{ABSTRACT_PUBMED_19020622}} | ||
==About this Structure== | ==About this Structure== | ||
[[3df0]] is a 3 chain structure with sequence 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]. | [[3df0]] is a 3 chain structure with sequence 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]. | ||
==See Also== | |||
*[[Calpain|Calpain]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:019020622</ref><ref group="xtra">PMID:011893336</ref><ref group="xtra">PMID:012665854</ref><ref group="xtra">PMID:010601010</ref><ref group="xtra">PMID:015491615</ref><references group="xtra"/> | ||
[[Category: Calpain-2]] | [[Category: Calpain-2]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: Green, D R.]] | [[Category: Green, D R.]] | ||
[[Category: Moldoveanu, T.]] | [[Category: Moldoveanu, T.]] | ||
[[Category: C2-like domain]] | [[Category: C2-like domain]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Inhibitor loop-out]] | [[Category: Inhibitor loop-out]] | ||
Revision as of 06:52, 20 October 2012
Calcium-dependent complex between m-calpain and calpastatin
Template:ABSTRACT PUBMED 19020622
About this Structure
3df0 is a 3 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- Moldoveanu T, Gehring K, Green DR. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Nature. 2008 Nov 20;456(7220):404-8. PMID:19020622 doi:10.1038/nature07353
- Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL. A Ca(2+) switch aligns the active site of calpain. Cell. 2002 Mar 8;108(5):649-60. PMID:11893336
- Moldoveanu T, Hosfield CM, Lim D, Jia Z, Davies PL. Calpain silencing by a reversible intrinsic mechanism. Nat Struct Biol. 2003 May;10(5):371-8. PMID:12665854 doi:10.1038/nsb917
- Hosfield CM, Elce JS, Davies PL, Jia Z. Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. EMBO J. 1999 Dec 15;18(24):6880-9. PMID:10601010 doi:10.1093/emboj/18.24.6880
- Moldoveanu T, Campbell RL, Cuerrier D, Davies PL. Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site. J Mol Biol. 2004 Nov 5;343(5):1313-26. PMID:15491615 doi:10.1016/j.jmb.2004.09.016
