Crystal structure of a complex of NOD1 CARD and ubiquitin.
basic_science · Level V
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- Record sourced from PubMed, PMID 25127239.
- Also identified by DOI 10.1371/journal.pone.0104017 and PMC identifier 4134136.
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Abstract
The Caspase Recruitment Domain (CARD) from the innate immune receptor NOD1 was crystallized with Ubiquitin (Ub). NOD1 CARD was present as a helix-swapped homodimer similar to other structures of NOD1 CARD, and Ub monomers formed a homodimer similar in conformation to Lys48-linked di-Ub. The interaction between NOD1 CARD and Ub in the crystal was mediated by novel binding sites on each molecule. Comparisons of these sites to previously identified interaction surfaces on both molecules were made along with discussion of their potential functional significance.
Medical subject headings
- Models, Molecular
- Nod1 Signaling Adaptor Protein
- Protein Conformation
- Protein Interaction Domains and Motifs
- Ubiquitin