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3df0

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[[Image:3df0.png|left|200px]]
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==About this Structure==
==About this Structure==
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3DF0 is a 3 chains 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].
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[[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].
==Reference==
==Reference==
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[[Category: Thiol protease]]
[[Category: Thiol protease]]
[[Category: Thiol protease inhibitor]]
[[Category: Thiol protease inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:19:10 2009''
 

Revision as of 21:16, 14 March 2011

Image:3df0.png

Template:STRUCTURE 3df0

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.

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
  • 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. The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):588-92. PMID:10639123
  • Todd B, Moore D, Deivanayagam CC, Lin GD, Chattopadhyay D, Maki M, Wang KK, Narayana SV. 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. J Mol Biol. 2003 Apr 18;328(1):131-46. PMID:12684003
  • 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

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