2p2c
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(New page: 200px<br /> <applet load="2p2c" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p2c, resolution 3.24Å" /> '''Inhibition of caspa...)
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Revision as of 21:13, 12 November 2007
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Inhibition of caspase-2 by a designed ankyrin repeat protein (DARPin)
Overview
Specific and potent caspase inhibitors are indispensable for the, dissection of the intricate pathways leading to apoptosis. We selected a, designed ankyrin repeat protein (DARPin) from a combinatorial library that, inhibits caspase-2 in vitro with a subnanomolar inhibition constant and, in contrast to the peptidic caspase inhibitors, with very high specificity, for this particular caspase. The crystal structure of this inhibitor, (AR_F8) in complex with caspase-2 reveals the molecular basis for the, specificity and, together with kinetic analyses, the allosteric mechanism, of inhibition. The structure also shows a conformation of the active site, that can be exploited for the design of inhibitory compounds. AR_F8 is a, specific inhibitor of an initiator caspase and has the potential to help, identify the function of caspase-2 in the complex biological apoptotic, signaling network.
About this Structure
2P2C is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Inhibition of Caspase-2 by a Designed Ankyrin Repeat Protein: Specificity, Structure, and Inhibition Mechanism., Schweizer A, Roschitzki-Voser H, Amstutz P, Briand C, Gulotti-Georgieva M, Prenosil E, Binz HK, Capitani G, Baici A, Pluckthun A, Grutter MG, Structure. 2007 May 16;15(5):625-636. PMID:17502107
Page seeded by OCA on Mon Nov 12 23:19:51 2007
