Figure 2
From: Late-onset spastic ataxia phenotype in a patient with a homozygous DDHD2 mutation
Structural consideration of an impact of the p.Val220Phe mutation in human DDHD2.
(A–B): A modeled structure of the region around Val220 in human DDHD2 (A) and the crystal structure of the catalytic domain of GPLRP2 chimerized with the C-terminal domain of HPL (PDB id; 1GPL) (B) are shown. The side chains of Val220 in A and the corresponding residue Ile74 in B are shown in red spheres. The catalytic triad in B and a component residue of the triad, Ser351, in A are shown in yellow spheres28. In A, a stretch of the sequence, Gly349-His-Ser-Leu352, which is conserved in most lipases22, is colored green and their side chains were shown as sticks, except for Ser351. Inset: close-up view of the squared region.
