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![[Figure 5]](mv5102fig5mag.jpg)
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Figure 5
Electrostatic surface potentials of NLRP14 PYD and the physiological D86V mutant reveal significant differences. (a) In NLRP14 PYD D86V the extensive negatively charged surface prominent in wild-type NLRP14 PYD is broken by hydrophobic patches. Interestingly, the possible interaction partner ASC presents a complementary charged surface around Arg41 suitable for interaction. (b) Proposed 2:1 complex model of NLRP14 PYD (chains A and B in pink and grey) and ASC PYD (PDB entry 1ucp, blue). Residues mediating the interaction are labelled and shown as sticks. This hypothetical model illustrates how the D86V mutation will affect the binding properties in the dimeric state of NLRP14 PYD. (c) NLRP14 PYD does not interact with ASC PYD in a 1:1 complex. NLRP14 PYD and the longer construct NLRP14 PYD+Linker were co-transformed with ASC. The SD/−Leu/−Trp plate confirms that the transformation worked for all combinations. However, the SD/−Ade/−His/−Leu/−Trp plate reveals that neither NLRP14 PYD nor NLRP14 PYD+Linker interacts with ASC PYD. In contrast, Aim2 PYD interacts with ASC in a 1:1 complex and thus demonstrates that the experimental setup worked. Lanes 1, 2, 3 and 4 indicate serial dilutions of 1:1, 1:10, 1:100 and 1:1000. |
![[Figure 5]](mv5102fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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