Fig. 3: The interaction between AK2 and αSyn is facilitated through the C-terminal region of αSyn, affecting widespread small structural changes on AK2, including the hinge region in particular.
From: Alpha-synuclein interacts with regulators of ATP homeostasis in mitochondria
a Intensity ratios of αSyn peaks in the presence and absence of AK2 extracted from 2D [15N,1H] HMQC NMR. A general decrease around the C-terminus indicates binding of this region to AK2. b Log2(fold change) of AK2 peptide (NGFLLDGFPR) proteolytic protection for αSyn monomer and ΔC-αSyn. c 2D [15N,1H] HMQC NMR spectrum of 150 μM 15N-labeled AK2 in the presence (blue) and absence (red) of 200 μM WT αSyn in PBS pH 7.5 at 25 °C. AK2 keeps its folded structure, however, many changes all over the spectrum can be seen. d Mapping the LiP-MS significant peptide of AK2 to its structure for interactions with WT αSyn monomer and ΔC-αSyn. The last panel shows the charge distribution of AK2. e, f Prediction of interaction between AK2 and αSyn. e Alpha-fold 2-based simulation of interactions between AK2 and WT αSyn. AK2 is shown in gray and αSyn in blue. In red is the AK2 peptide that changes in structure in the LiP-MS experiment. Portions of this peptide are at the predicted interaction interface. f Mapping the predicted interaction interface of AK2 on the sequence of αSyn. Source data are provided as a Source Data file.
