7VTP

Cryo-EM structure of PYD-deleted human NLRP3 hexamer

7VTP の概要

• エントリーDOI: 10.2210/pdb7vtp/pdb
• EMDBエントリー: 32119
• 分子名称: NACHT, LRR and PYD domains-containing protein 3, ADENOSINE-5'-DIPHOSPHATE, 1-[4-(2-oxidanylpropan-2-yl)furan-2-yl]sulfonyl-3-(1,2,3,5-tetrahydro-s-indacen-4-yl)urea (3 entities in total)
• 機能のキーワード: nlr, nod-like receptor, nlrp3, inflammasome, immune system
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 642769.22

構造登録者

Ohto, U.,Shimizu, T. (登録日: 2021-10-30, 公開日: 2022-03-09, 最終更新日: 2024-06-26)

主引用文献

Ohto, U.,Kamitsukasa, Y.,Ishida, H.,Zhang, Z.,Murakami, K.,Hirama, C.,Maekawa, S.,Shimizu, T.
Structural basis for the oligomerization-mediated regulation of NLRP3 inflammasome activation.
Proc.Natl.Acad.Sci.USA, 119:e2121353119-e2121353119, 2022

PubMed Abstract: SignificanceThe nucleotide-binding oligomerization domain (NOD)-like receptor pyrin domain containing 3 (NLRP3) is a pattern recognition receptor that forms an inflammasome. The cryo-electron microscopy structure of the dodecameric form of full-length NLRP3 bound to the clinically relevant NLRP3-specific inhibitor MCC950 has established the structural basis for the oligomerization-mediated regulation of NLRP3 inflammasome activation and the mechanism of action of the NLRP3 specific inhibitor. The inactive NLRP3 oligomer represents the NLRP3 resting state, capable of binding to membranes and is likely disrupted for its activation. Visualization of the inhibitor binding mode will enable optimization of the activity of NLRP3 inflammasome inhibitor drugs.

PubMed: 35254907
DOI: 10.1073/pnas.2121353119

実験手法

ELECTRON MICROSCOPY (3.23 Å)