Extended Data Fig. 3: Distribution of ASM enzymatic activity levels of rare SMPD1 variants in relation to protein ___domain localisation and tertiary structure integrity. | Nature Aging

Extended Data Fig. 3: Distribution of ASM enzymatic activity levels of rare SMPD1 variants in relation to protein ___domain localisation and tertiary structure integrity.

From: Exome sequencing in Asian populations identifies low-frequency and rare coding variation influencing Parkinson’s disease risk

Extended Data Fig. 3

(a) Each rare SMPD1 variant was classified by its localization to protein domains across the ASM protein, namely the signalling peptide (12 variants), saponin (12 variants), proline linker (7 variants), metallophosphate (70 variants), and C terminus (19 variants). (b) Each rare SMPD1 variant was classified by its effect on ASM protein tertiary structure integrity as benign (15 variants), deleterious (27 variants) and uncertain (7 variants). Analysis for both panels are based on protein crystallography of ASM tertiary structure (PDB: 5i81). Median, 25th-75th quartiles, whiskers of 1.5× IQR shown in boxplot. Two-sided t-test: P < 0.05 indicated by *, P < 0.01 indicated by **; P < 0.001 indicated by ***.

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