4I16

Crystal structure of CARMA1 CARD

Summary for 4I16

• Entry DOI: 10.2210/pdb4i16/pdb
• Descriptor: Caspase recruitment domain-containing protein 11, SULFATE ION (3 entities in total)
• Functional Keywords: cbm complex, helix bundle, scaffold protein, bcl10 and malt1 binding, phosphorylation, signaling protein
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm (By similarity): Q8CIS0
• Total number of polymer chains: 1
• Total formula weight: 11240.71

Authors

Li, S.,Yang, X.,Shen, Y. (deposition date: 2012-11-20, release date: 2012-12-26, Last modification date: 2024-03-20)

Primary citation

Li, S.,Yang, X.,Shao, J.,Shen, Y.
Structural insights into the assembly of CARMA1 and BCL10
Plos One, 7:e42775-e42775, 2012

PubMed Abstract: The CBM complex (CARMA1, BCL10 and MALT1) plays a crucial role in B and T lymphocyte activation. CARMA1 serves as a scaffold for BCL10, MALT1 and other effector proteins and regulates various signaling pathways related to the immune response. The assembly of CARMA1 and BCL10 is mediated through a CARD-CARD interaction. Here, we report the crystal structure of the CARD domain of CARMA1 at a resolution of 1.75 Å. The structure consists of six helices, as previously determined for CARD domains. Structural and computational analysis identified the binding interface between CARMA1-CARD and BCL10-CARD, which consists of a basic patch in CARMA1 and an acidic patch in BCL10. Site-directed mutagenesis, co-immunoprecipitation and an NF-κB activation assay confirmed that the interface is necessary for association and downstream signaling. Our studies provide molecular insight into the assembly of CARMA1 and BCL10.

PubMed: 22880103
DOI: 10.1371/journal.pone.0042775

Experimental method

X-RAY DIFFRACTION (1.751 Å)