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![[Figure 1]](mv5102fig1mag.jpg)
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Figure 1
Symmetric dimerization of NLRP14 PYD mediated by an extended α5/6 helix. (a) The crystal structure of the wild-type NRLP14 PYD is viewed along the molecular twofold axis (chain A in pink; chain B in light grey); the important hydrophobic side chains Trp72, Leu76 and Leu87 are shown in stick representation, highlighting their contribution to symmetric α5/6A–α5/6B binding. (b) The crystal structure of the physiologically relevant D86V mutant (chain A in magenta; chain B in dark grey) is superimposed onto the virtually identical structure of wild-type NLRP14 PYD (chain A in pink; chain B in light grey). Additionally, a model of the canonical six-helix bundle conformation is superimposed (cyan), identifying the conformationally adaptive role of Trp72, Leu76 and Leu87, which can either engage in symmetric dimerization (extended α5/6 stem-helix conformation) or in stabilization of the hydrophobic core (canonical closed conformation). (c) Enlarged view of the dimer interface, showing that a variety of hydrophobic, polar and charged interactions stabilize the dimer interface. Dimer contacts are not limited to α5/6A–α5/6B interactions, as exemplified by the monodentate and bidentate interactions of Arg90 (α5/6B) with Glu21 (α1A) and Glu26 (α2A), respectively. |
![[Figure 1]](mv5102fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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