Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment.
摘要：
Apoptosis requires recruitment of caspases by receptor-associated adaptors through homophilic interactions between the CARDs (spase ecruitment omains) of adaptor proteins and prodomains of caspases. We have solved the CARD structure of the RAIDD adaptor protein that recruits ICH-1/caspase-2. It consists of six tightly packed helices arranged in a topology homologous to the Fas death domain. The surface contains a basic and an acidic patch on opposite sides. This polarity is conserved in the ICH-1 CARD as indicated by homology modeling. Mutagenesis data suggest that these patches mediate CARD/CARD interaction between RAIDD and ICH-1. Subsequent modeling of the CARDs of Apaf-1 and caspase-9, as well as Ced-4 and Ced-3, showed that the basic/acidic surface polarity is highly conserved, suggesting a general mode for CARD/CARD interaction.
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关键词：
Cysteine Endopeptidases Caspases Proteins Carrier Proteins Crystallography, X-Ray Nuclear Magnetic Resonance, Biomolecular Sequence Alignment Mutagenesis Amino Acid Sequence Protein Conformation
DOI：
10.1016/S0092-8674(00)81417-8
被引量：
年份：
1998
Elsevier
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万方医学
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