Crystal structure of a complex of NOD1 CARD and ubiquitin

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

doi:10.1371/journal.pone.0104017

Crystal structure of a complex of NOD1 CARD and ubiquitin

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

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

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.

Original language	English
Article number	e104017
Journal	PloS one
Volume	9
Issue number	8
DOIs	https://doi.org/10.1371/journal.pone.0104017
State	Published - Aug 15 2014

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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.",

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AU - Gakhar, Lokesh

AU - Piper, Robert C.

AU - Subramanian, Ramaswamy

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AB - 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.

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Crystal structure of a complex of NOD1 CARD and ubiquitin

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