Structural highlights
Publication Abstract from PubMed
Nod-like receptors (NLRs), Nod1 and Nod2 are cytosolic detectors of pathogen-associated molecular patterns (PAMPs). Nod1 is a three-domain protein, consisting of a caspase activation and recruitment domain (CARD), a nucleotide-binding oligomerization domain (NOD), and a leucine-rich repeat domain (LRR). The binding of PAMPs to the LRR results in the activation of signaling through homophilic CARD-CARD interactions. Several CARD structures have been determined, including a recent NMR structure of Nod1 CARD. In contrast to the reported NMR structure, the crystal structure reported here is a dimer, where the sixth helix is swapped between two monomers. While the overall structure is very similar to the known CARD structures, this is the first report of a homodimeric CARD structure. The ability of the CARD to exist in monomeric and dimeric forms suggests another level of regulation in the activation of NLR proteins.
Crystal structure of the Nod1 caspase activation and recruitment domain.,Coussens NP, Mowers JC, McDonald C, Nunez G, Ramaswamy S Biochem Biophys Res Commun. 2007 Feb 2;353(1):1-5. Epub 2006 Dec 6. PMID:17173864[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Coussens NP, Mowers JC, McDonald C, Nunez G, Ramaswamy S. Crystal structure of the Nod1 caspase activation and recruitment domain. Biochem Biophys Res Commun. 2007 Feb 2;353(1):1-5. Epub 2006 Dec 6. PMID:17173864 doi:S0006-291X(06)02513-7