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1tl9
From Proteopedia
(Difference between revisions)
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| - | {{Seed}} | ||
[[Image:1tl9.png|left|200px]] | [[Image:1tl9.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1tl9]] is a 2 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=1TL9 OCA]. | |
==Reference== | ==Reference== | ||
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[[Category: Moldoveanu, T.]] | [[Category: Moldoveanu, T.]] | ||
[[Category: Covalently-linked inhibitor at the active site cysteine forms a hemithioacetal]] | [[Category: Covalently-linked inhibitor at the active site cysteine forms a hemithioacetal]] | ||
| - | + | [[Category: Hydrolase]] | |
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Revision as of 20:17, 14 March 2011
High resolution crystal structure of calpain I protease core in complex with leupeptin
Template:ABSTRACT PUBMED 15491615
About this Structure
1tl9 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
- 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
- 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
