Supplementary Figure 10: Amide secondary chemical shifts of rdHDL and structural clustering of functionally relevant familial mutations of apoA-I. | Nature Structural & Molecular Biology

Supplementary Figure 10: Amide secondary chemical shifts of rdHDL and structural clustering of functionally relevant familial mutations of apoA-I.

From: Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I

Supplementary Figure 10

(a) Residues with a positive amide secondary chemical shift Δδ1HN (see Fig 4 in main text) are colored yellow on top of a surface representation of the 3D structure of rdHDL, which is cut in half to show the interior. The surface representation of the conformer with the lowest CYANA target function is shown. A positive amide secondary chemical shift Δδ1HN is indicative of a shorter hydrogen bond, which is expected to be located in the inner side of the MSPΔH5 molecules of the rdHDL. (b) A surface representation of the 3D structure of the rdHDL is shown. Known apoA-I mutations that do not affect HDL plasma concentrations are mapped onto the upper apoA-I molecule in blue, while mutations affecting HDL plasma concentrations are mapped in red that cluster structurally.

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