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The structural and biochemical analysis of homodimerization of caspase-recruitment domain of Nod1 (Nod1_CARD), an essential cytoplasmic sensor for bacterial peptidoglycans in the innate immune system is reported. The results shed light into the pH-sensitive monomer/dimer transition which is a unique property of Nod1_CARD.

Effects of organic solvents on all beta-sheet protein are investigated to understand the influence of backbone conformation on protein aggregation. It also gives strategies to prevent vitro and in vitro protein aggregation and it is found that protein aggregation is accompanied by the formation of non-native beta-sheet conformation.

The caspase-recruitment domain (CARD) is known to play an important role in apoptosis and inflammation as an essential protein–protein interaction domain. The CARD of the cytosolic pathogen receptor Nod1 was overexpressed in Escherichia coli and purified by affinity chromatography and gel filtration. The purified CARD was crystallized at 277 K using the microseeding method. X-ray diffraction data were collected to 1.9 Å resolution. The crystals belong to space group P31 or P32, with unit-cell parameters a = b = 79.1, c = 80.9 Å. Preliminary analysis indicates that there is one dimeric CARD molecule in the asymmetric unit. [ABSTRACT FROM AUTHOR]