Crystal Structure of the Nod1 Caspase Activation and Recruitment Domain.
From: Department of Biochemistry, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA, USA.
Biochemical and biophysical research communications
- Publish Date: Feb 2007
- ISSN: 0006-291X
- Volume: 353
- Issue: 1
- Pages: 1-5
- Medium: Print
- Language: English
- Citation (JAMA): Coussens Nathan P, Mowers Jonathan C, McDonald Christine, et al. Crystal Structure of the Nod1 Caspase Activation and Recruitment Domain.. Biochem. Biophys. Res. Commun. Feb 2007;353:1-5
Abstract
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.
Mesh Headings (Keywords): Binding Sites, Caspases, Crystallography, Enzyme Activation, Leucine, Models, Chemical, Models, Molecular, Nod1 Signaling Adaptor Protein, Protein Binding, Protein Conformation, Protein Structure, Tertiary
Check for Full Text / PubMed Unique Identifier (PMID): 17173864
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