5IRN
Crystal structure of rabbit NOD2 in an ADP-bound state (Crystal form1)
Summary for 5IRN
| Entry DOI | 10.2210/pdb5irn/pdb |
| Related | 5IRL 5IRM |
| Descriptor | Uncharacterized protein, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | immune system, nod2, innate immunity |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 92305.90 |
| Authors | Maekawa, S.,Ohto, U.,Shimizu, T. (deposition date: 2016-03-14, release date: 2016-06-29, Last modification date: 2024-03-20) |
| Primary citation | Maekawa, S.,Ohto, U.,Shibata, T.,Miyake, K.,Shimizu, T. Crystal structure of NOD2 and its implications in human disease. Nat Commun, 7:11813-11813, 2016 Cited by PubMed Abstract: Nucleotide-binding oligomerization domain-containing protein 2 (NOD2), a member of the NOD-like receptors family, are crucial for innate immune responses. Mutations of NOD2 have been associated with chronic inflammatory disorders such as Crohn's disease (CD), Blau syndrome (BS) and early-onset sarcoidosis (EOS), but little is known about its signalling mechanism and the role it plays in these diseases. Here, we report the crystal structure of rabbit NOD2 in an ADP-bound state. The structure reveals an inactive closed conformation in which the subdomains in the NOD domain are closely packed by ADP-mediated and inter-domain interactions. Mapping of the BS- or EOS-associated gain-of-function mutations reveals that most of these mutations are located in the NOD subdomain interfaces, and are likely to disrupt the inner domain interactions, facilitating a conformational change to the active form. Conversely, mutations associated with CD are distributed throughout the protein, some of which may affect oligomer formation and ligand binding. PubMed: 27283905DOI: 10.1038/ncomms11813 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.34 Å) |
Structure validation
Download full validation report
