3df0

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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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<ref group="xtra">PMID:19020622</ref><ref group="xtra">PMID:11893336</ref><ref group="xtra">PMID:12665854</ref><ref group="xtra">PMID:10601010</ref><ref group="xtra">PMID:10639123</ref><ref group="xtra">PMID:12684003</ref><ref group="xtra">PMID:15491615</ref><references group="xtra"/>
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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]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10601010 10601010]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10639123 10639123]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12684003 12684003]
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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]
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[[Category: Calpain-2]]
[[Category: Calpain-2]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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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 Dec 10 15:51:24 2008''
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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 12:19, 16 February 2009

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

  • 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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