Fig. 1
From: Newly discovered roles of triosephosphate isomerase including functions within the nucleus
Structure of the human TPI protein homodimer with selected residues displayed. A Several key amino acids (magenta) are labeled that cause or model disease. The TPIE105 substitution site, which is associated with nearly all cases of human TPI deficiency, is noted. Also noted are the TPIQ181 and TPII171 mutation sites which only cause disease when paired with a TPI1E105D allele. Finally, the TPIM83 mutation site in the human TPI protein, which corresponds to the Drosophila TPIsgk mutation site, is shown. Important to note is the proximity of both the TPIE105 and TPIM83 residues to the dimer interface. B Active site residues and the TPIS80 phosphorylation site. Active site residues TPIK14, TPIH96, and TPIE166 are displayed in orange. The TPIS80 phosphorylation site, which affects the nuclear localization of TPI, is displayed in red. The TPIS80 phosphorylation site is labeled on the opposite subunit as the active site residues are labeled. Figure created with the PyMOL Molecular Graphics System, Version 2.5.2, Schrödinger, LLC, using Protein Data Bank structure 4POC