Crystal Structure of a Complex of NOD1 CARD and Ubiquitin

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 interact...

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Autores principales: Ver Heul, Aaron M., Gakhar, Lokesh, Piper, Robert C., Subramanian, Ramaswamy
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4134136/
https://www.ncbi.nlm.nih.gov/pubmed/25127239
http://dx.doi.org/10.1371/journal.pone.0104017
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author Ver Heul, Aaron M.
Gakhar, Lokesh
Piper, Robert C.
Subramanian, Ramaswamy
author_facet Ver Heul, Aaron M.
Gakhar, Lokesh
Piper, Robert C.
Subramanian, Ramaswamy
author_sort Ver Heul, Aaron M.
collection PubMed
description 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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spelling pubmed-41341362014-08-19 Crystal Structure of a Complex of NOD1 CARD and Ubiquitin Ver Heul, Aaron M. Gakhar, Lokesh Piper, Robert C. Subramanian, Ramaswamy PLoS One Research Article 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. Public Library of Science 2014-08-15 /pmc/articles/PMC4134136/ /pubmed/25127239 http://dx.doi.org/10.1371/journal.pone.0104017 Text en © 2014 Ver Heul et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Ver Heul, Aaron M.
Gakhar, Lokesh
Piper, Robert C.
Subramanian, Ramaswamy
Crystal Structure of a Complex of NOD1 CARD and Ubiquitin
title Crystal Structure of a Complex of NOD1 CARD and Ubiquitin
title_full Crystal Structure of a Complex of NOD1 CARD and Ubiquitin
title_fullStr Crystal Structure of a Complex of NOD1 CARD and Ubiquitin
title_full_unstemmed Crystal Structure of a Complex of NOD1 CARD and Ubiquitin
title_short Crystal Structure of a Complex of NOD1 CARD and Ubiquitin
title_sort crystal structure of a complex of nod1 card and ubiquitin
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4134136/
https://www.ncbi.nlm.nih.gov/pubmed/25127239
http://dx.doi.org/10.1371/journal.pone.0104017
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