2h51: Difference between revisions
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[[Image:2h51.png|left|200px]] | [[Image:2h51.png|left|200px]] | ||
{{STRUCTURE_2h51| PDB=2h51 | SCENE= }} | {{STRUCTURE_2h51| PDB=2h51 | SCENE= }} | ||
===Crystal structure of human caspase-1 (Glu390->Asp and Arg286->Lys) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)=== | ===Crystal structure of human caspase-1 (Glu390->Asp and Arg286->Lys) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)=== | ||
{{ABSTRACT_PUBMED_18590738}} | {{ABSTRACT_PUBMED_18590738}} | ||
Revision as of 23:28, 26 July 2012
Crystal structure of human caspase-1 (Glu390->Asp and Arg286->Lys) in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)
Template:ABSTRACT PUBMED 18590738
About this Structure
2h51 is a 3 chain structure of Caspase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Datta D, Scheer JM, Romanowski MJ, Wells JA. An allosteric circuit in caspase-1. J Mol Biol. 2008 Sep 19;381(5):1157-67. Epub 2008 Jun 20. PMID:18590738 doi:10.1016/j.jmb.2008.06.040
- Fang B, Boross PI, Tozser J, Weber IT. Structural and kinetic analysis of caspase-3 reveals role for s5 binding site in substrate recognition. J Mol Biol. 2006 Jul 14;360(3):654-66. Epub 2006 Jun 2. PMID:16781734 doi:10.1016/j.jmb.2006.05.041