ArticlePloS one2013
Novel disulfide bond-mediated dimerization of the CARD domain was revealed by the crystal structure of CARMA1 CARD.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Assembly of platforms for signal transduction in the new era: dimerization, helical filament assembly, and beyond.Experimental & molecular medicine · 2020Review
- Caspase recruitment domains for protein interactions in cellular signaling (Review).International journal of molecular medicine · 2019Article
- Molecular architecture and regulation of BCL10-MALT1 filaments.Nature communications · 2018Article
- Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction.PloS one · 2018Article
- Mechanisms of Regulated and Dysregulated CARD11 Signaling in Adaptive Immunity and Disease.Frontiers in immunology · 2018Review
- Crystal structure of caspase recruiting domain (CARD) of apoptosis repressor with CARD (ARC) and its implication in inhibition of apoptosis.Scientific reports · 2015Article
- An updated view on the structure and function of PYRIN domains.Apoptosis : an international journal on programmed cell death · 2015Article
- Crystallization and preliminary X-ray crystallographic analysis of the CARD domain of apoptosis repressor with CARD (ARC).Acta crystallographica. Section F, Structural biology communications · 2015Article
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Authors and funding
3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
CARMA1, BCL10 and MALT1 form a large molecular complex known as the CARMA1 signalosome during lymphocyte activation. Lymphocyte activation via the CARMA1 signalosome is critical to immune response and linked to many immune diseases. Despite the important role of the CARMA1 signalosome during lymphocyte activation and proliferation, limited structural information is available. Here, we report the dimeric structure of CARMA1 CARD at a resolution of 3.2 Å. Interestingly, although CARMA1 CARD has a canonical six helical-bundles structural fold similar to other CARDs, CARMA1 CARD shows the first homo-dimeric structure of CARD formed by a disulfide bond and reveals a possible biologically important homo-dimerization mechanism.
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