2NSN

Crystal structure of Caspace Activation and Recruitment Domain (CARD) of NOD1

2NSN の概要

• エントリーDOI: 10.2210/pdb2nsn/pdb
• 関連するPDBエントリー: 1CY5 1DGN 2B1W 3CRD 3YGS
• 分子名称: Caspase recruitment domain-containing protein 4 (2 entities in total)
• 機能のキーワード: six helix greek key motif, apoptosis
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q9Y239
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10977.56

構造登録者

Ramaswamy, S.,Coussens, N.P. (登録日: 2006-11-05, 公開日: 2006-12-19, 最終更新日: 2023-08-30)

主引用文献

Coussens, N.P.,Mowers, J.C.,McDonald, C.,Nunez, G.,Ramaswamy, S.
Crystal structure of the Nod1 caspase activation and recruitment domain.
Biochem.Biophys.Res.Commun., 353:1-5, 2007

PubMed Abstract: Nod-like receptors (NLRs), Nod1 and Nod2 are cytosolic detectors of pathogen-associated molecular patterns (PAMPs). Nod1 is a three-domain protein, consisting of a caspase activation and recruitment domain (CARD), a nucleotide-binding oligomerization domain (NOD), and a leucine-rich repeat domain (LRR). The binding of PAMPs to the LRR results in the activation of signaling through homophilic CARD-CARD interactions. Several CARD structures have been determined, including a recent NMR structure of Nod1 CARD. In contrast to the reported NMR structure, the crystal structure reported here is a dimer, where the sixth helix is swapped between two monomers. While the overall structure is very similar to the known CARD structures, this is the first report of a homodimeric CARD structure. The ability of the CARD to exist in monomeric and dimeric forms suggests another level of regulation in the activation of NLR proteins.

PubMed: 17173864
DOI: 10.1016/j.bbrc.2006.11.122

実験手法

X-RAY DIFFRACTION (2 Å)