New protein structures to aid rational drug design tamu NatureComms
-1” as the dominant mode of DAG binding to C1Bδ. Moreover, also consistent with the C1Bδ-DAG structure, several C1Bδ loop residues show NOEs to the methylenes of acyl chains of either DAG or bicelle lipids .Inspection of C1Bδ loop regions in the C1Bδ-DAG structure reveals how exquisitely they are tuned to the chemical properties of diacylglycerol and surrounding lipids.
Pro241, a strictly conserved residue in DAG-sensitive C1 domains, makes non-polar contacts with the C2 carbon of DAG, and its Cδ/Cα are positioned sufficiently close to the DAG oxygens to form C–H…O interactions . On the opposite side of the groove, the polar N–H group of Gly253 hydrogen bonds to the O5 oxygen, while the hydrophobic Leu250 sidechain engages in non-polar contacts with the C1 carbon of DAG.
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