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Extended Data Fig. 5: The structure of the NLRP3–NEK7 complex, showing the modelled full-length NEK7 and NLRP3 domain comparisons. | Nature

Extended Data Fig. 5: The structure of the NLRP3–NEK7 complex, showing the modelled full-length NEK7 and NLRP3 domain comparisons.

From: Structural mechanism for NEK7-licensed activation of NLRP3 inflammasome

Extended Data Fig. 5

a, Two views of the NLRP3–NEK7 complex structure with the NEK7 N-lobe (grey) modelled from the NEK7 crystal structure (PDB code 2WQM). b, The disordered activation loop, including S195 in the NLRP3–NEK7 complex, which is not involved in NLRP3 interaction. c, NBD, HD1, WHD and HD2 of NLRP3, NOD2 (PDB code 5IRL) and NLRC4 (PDB code 4KXF) superimposed and shown side-by-side for comparison. d, e, NOD2 (d) and NLRC4 (e) structures6,21 in inactive conformations and in the orientation of NLRP3 (shown in a) by superposing on the NBD and HD1 domains. The location of phosphorylated S533 of NLRC4 is labelled.

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