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. Author manuscript; available in PMC: 2012 Nov 4.
Published in final edited form as: J Mol Biol. 2011 Sep 28;413(4):790–803. doi: 10.1016/j.jmb.2011.09.024

Figure 6.

Figure 6

Mapping the interaction of NLRP12 PYD with FAF-11–57. (A) Chemical shift perturbations (CSPs) calculated for NLRP12 PYD upon titration of FAF-11–57 at a molar ratio of 1:10 (10 mM Na-phosphate buffer pH 7.0, 100 mM NaCl, 0.5 mM TCEP). The color scheme denotes the intensity of the shifts observed in the titration experiment. CSP values higher than two standard deviations from the mean are colored light blue; three standard deviations, marine; and four standard deviations, purple. Experimentally derived secondary structure elements of NLRP12 PYD are depicted by grey cylinders on top of the figure. (B) NLRP12 PYD structure displaying the residues that show the highest CSP values upon titration with FAF-11–57. Side chains are depicted in stick model, labeled and colored according to A. (C) Surface representation of the NLRP12 PYD structure in the same orientation as B, displaying the residues that show the highest CSP values. These residues are clustered on the α2-α3 surface, which has been previously implicated in homotypic interactions of PYDs.