NLRP10 is a special member of NOD-like receptors (NLRs) family that lacks the leucine-rich repeats, suggesting that NLRP10 may act as an immunity regulator rather than directly receptor recognizing intracellular pathogen products. Previous studies on NLRP10 show that NLRP10 can interact with several components of NOD1 pathway thereby enhancing NOD1-mediated innate immune responses. In particular models, NLRP10 also negatively affects the activation of NLRP3 inflammasome. It has been proposed that NLRP10 oligomers interact with ASC to form a multi-protein platform for the recruitment of caspase-1 or other signaling components. Here, we show that pyrin-like domain (PYD) degradation induce the formation of NLRP10 oligomers, which present stick-shaped and circular structure. With the NLRP10 mutant G173A made by means of site-directed mutagenesis, we successfully obtain homogeneous full-length NLRP10 preparations. Corresponding gel filtration analysis and electron microscope (EM) data further proved that the PYD domain is important in protecting NLRP10 against aggregation.