Table 3.
Docking-based characterization of HADHA mutations.
| UniProt 1 (Partner) | Neutral Mutations | Pathogenic Mutations 2 | ||
|---|---|---|---|---|
| Core 3 | Rim 3 | Core 3 | Rim 3 | |
| O95166 | D398G | A396G, K406R | - | R399 *, V412L |
| P60520 | - | D398G, K406R | - | R399 *, V412L |
| Q14164 | D398G | A396G, K406R, K519R, A596V, S654N, K734Q | - | Q358K, R399 *, V412L, R610G, Y740 * |
| Q99714 | D398G, S654N | A396G, K406R, A596V, R645S, R645N, L661I, K734Q | - | R399 *, V412L, R610G, Y740 * |
| Q9GZQ8 | D398G | V52I, V526I, N142S, L221I, E223T, I237M, A396G, K406R | - | R399 *, V412L |
| Q9H0R8 | D398G | N142S, L221I, E223T, I237M, A396G, K406R, S654N, L661I | - | R399 *, V412L |
1 UniProt code of the corresponding interacting partner. 2 The symbol “*” indicates stop codon. Mutations R399*, Y740* and V412L (in bold) are associated with mitochondrial trifunctional protein deficiency. Mutation Q358K (in italics) is associated to haemolysis, elevated liver enzymes, and low platelets. Mutation R610G is associated to long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. 3 Interface core and rim estimated from the docking calculations.