7VTQ
Cryo-EM structure of mouse NLRP3 (full-length) dodecamer
Summary for 7VTQ
| Entry DOI | 10.2210/pdb7vtq/pdb |
| EMDB information | 32120 |
| Descriptor | 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) |
| Functional Keywords | nlr, nod-like receptor, nlrp3, inflammasome, immune system |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 12 |
| Total formula weight | 1466947.70 |
| Authors | Ohto, U.,Shimizu, T. (deposition date: 2021-10-30, release date: 2022-03-09, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 35254907DOI: 10.1073/pnas.2121353119 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.55 Å) |
Structure validation
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