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Fig. 7 | Molecular Autism

Fig. 7

From: Biophysical classification of a CACNA1D de novo mutation as a high-risk mutation for a severe neurodevelopmental disorder

Fig. 7

Molecular modeling of Cav1.3 WT α1-subunits, mutations S652L and S652W. Top: Top view and side view of the Cav1.3 α1-subunit structure. The region involving the inter-domain interactions (IIS4-S5–IS4-IS5) affected by the mutation is highlighted (left). Bottom: a WT inter-domain interaction of S652 in repeat II and S256 in the S4-S5 linker in repeat I. b Weaker hydrophobic interactions of the mutated residue L652 with the hydrophobic cloud in the S4-S5 linker of repeat I. c Stabilizing effect of the W652 mutation; the tryptophan residue can form an intra-domain hydrogen bond with the backbone of K648 and due to its aromatic character an inter-domain pi-H interaction with S256.

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