Fig. 2: The recognition of InsP6 by the ___domain-swapped rice SPX2 dimer in the SPX2/InsP6/PHR2 complex. | Nature Communications

Fig. 2: The recognition of InsP6 by the ___domain-swapped rice SPX2 dimer in the SPX2/InsP6/PHR2 complex.

From: Mechanistic insights into the regulation of plant phosphate homeostasis by the rice SPX2 – PHR2 complex

Fig. 2

a Binding surface of InsP6 in the SPX2 dimer. b The electrostatic surface of the InsP6 binding surface, colored in terms of electrostatic potential, and displayed in a scale from red (−5 kT/e) to blue (+5 kT/e). c Co-expression coupled Ni-NTA pull-down assess the InsP6-binding dependent SPX2–PHR2 association. Experiments were independently repeated three times with similar results. d Interface of the SPX2 dimer. PHR2 has been omitted for clearity. e Co-expression coupled Ni-NTA pull-down assess the SPX2 dimerization for SPX2/PHR2 association. Experiments were independently repeated three times with similar results. For the pull-down assay, different mutated versions of the full length SPX21–280 and His-tagged PHR2225–362 were co-expressed in the presence of 1 mM InsP6.

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