5IRM

Crystal structure of rabbit NOD2 in an ADP-bound state (Crystal form2)

5IRM の概要

• エントリーDOI: 10.2210/pdb5irm/pdb
• 関連するPDBエントリー: 5IRL 5IRN
• 分子名称: Uncharacterized protein, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: immune system, nod2, innate immunity
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 184611.79

構造登録者

Maekawa, S.,Ohto, U.,Shimizu, T. (登録日: 2016-03-14, 公開日: 2016-06-29, 最終更新日: 2024-03-20)

主引用文献

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

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: 27283905
DOI: 10.1038/ncomms11813

実験手法

X-RAY DIFFRACTION (3.31 Å)