Crystal structure of a complex of NOD1 CARD and ubiquitin

Aaron M. Ver Heul, Lokesh Gakhar, Robert C. Piper, Ramaswamy Subramanian

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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.

Original languageEnglish
Article numbere104017
JournalPloS one
Issue number8
StatePublished - Aug 15 2014


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