1tl9
From Proteopedia
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[[Image:1tl9.png|left|200px]] | [[Image:1tl9.png|left|200px]] | ||
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{{STRUCTURE_1tl9| PDB=1tl9 | SCENE= }} | {{STRUCTURE_1tl9| PDB=1tl9 | SCENE= }} | ||
===High resolution crystal structure of calpain I protease core in complex with leupeptin=== | ===High resolution crystal structure of calpain I protease core in complex with leupeptin=== | ||
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{{ABSTRACT_PUBMED_15491615}} | {{ABSTRACT_PUBMED_15491615}} | ||
==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]. | [[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]. | ||
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| + | ==See Also== | ||
| + | *[[Calpain|Calpain]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:015491615</ref><ref group="xtra">PMID:011893336</ref><ref group="xtra">PMID:012665854</ref><references group="xtra"/> |
[[Category: Calpain-1]] | [[Category: Calpain-1]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[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]] | [[Category: Hydrolase]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
Revision as of 16:22, 20 October 2012
Contents |
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.
See Also
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
