Fig. 4: A variable region of MBOAT7 TM segments 4 and 5 determines the selectivity towards lysophospholipid substrates. | Nature Communications

Fig. 4: A variable region of MBOAT7 TM segments 4 and 5 determines the selectivity towards lysophospholipid substrates.

From: The structure of phosphatidylinositol remodeling MBOAT7 reveals its catalytic mechanism and enables inhibitor identification

Fig. 4

a Sequence alignment of MBOAT1, 5 and 7 from different species. Only the variable regions and the short flank sequences are shown. The full sequence alignment can be seen in Supplementary Fig. 8. Conserved residues are highlighted with gray shadow. The key residues for recognizing the specific headgroups were colored. The swapping regions are also indicated. b The overlay of pockets for the lyso-phospholipid headgroups from MBOAT1, 2 and 5. The highly conserved residues from TM9 and 10 are shown in gray, and the variable regions are shown in different colors. c The detailed interaction between MBOAT and their specific phospholipid headgroups. The colors are consistent with b. 3PS, 3-phosphorylserine; 3PC, 3-phosphorylcholine; 3PI, 3-phosphorylinositol. d, e The activity analysis of the region-swapped chimeric proteins. Protein levels were adjusted to the immunoblotting against GFP (upper). The activity is detected by the production of radioactive PI (d) or PC (e) on a TLC. The experiments were independently performed 3 times with similar results. Source data are provided as a Source Data file.

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