Figure 5.

A structural model of BIN2. Shown here are two rotational (0° and 60°) views of a modeled BIN2 structure obtained at SWISS-MODEL (https://swissmodel.expasy.org/). Individual β-strands (β1-β5) and α-helices (αC-αH) were labeled. The two extra antiparallel-β-strands that cap the N-lobe are not labelled. The TREE motif and the Pro²⁸⁴ residue mutated in known bin2/dwarf12/ucu1 alleles are indicated with grey-colored sticks. The magenta sticks show the three positively charged residues [Arg⁸⁰, Arg¹⁶⁴, and Lys¹⁸⁹ (also acetylated)] of the conserved phosphate-binding pocket, the red sticks with red dots denote the Tyr²⁰⁰ residue, the green sticks with green dots mark the Lys⁶⁹-Glu⁸¹ salt bridge between the β3-strand and the αC-helix, and the blue sticks represent the Lys¹⁶⁷ residue that corresponds to the acetylated Lys¹⁸³ residue of the human GSK3β. The red spheres show the Cys residues that were shown to be S-nitrosylated or S-glutathionylated in vitro, the orange spheres indicate the gatekeeper Met¹¹⁵ residue, and the pink spheres mark the 5 R-spine residues (from lower to top: Asp²²³, His¹⁶³, Phe¹⁸⁵, Met⁸⁵, and Leu⁹⁶). Important residues are also labelled with single letter codes with positions. The rainbow bar indicates the order of AAs from the N-terminus (blue) to the C-terminus (red).