Results: 4

1.
Fig. 4

Fig. 4. From: The genotypic and phenotypic spectrum of pyridoxine-dependent epilepsy due to mutations in ALDH7A1.

Overview of pyridoxine dependent/responsive seizure subtypes. Possible mutations associated with group 1 include T297R, IVS-16(+5)G>A, and c.1512delG

Gunter Scharer, et al. J Inherit Metab Dis. ;33(5):571-581.
2.
Fig. 3

Fig. 3. From: The genotypic and phenotypic spectrum of pyridoxine-dependent epilepsy due to mutations in ALDH7A1.

Mapped locations of missense mutations associated with pyridoxine-dependent epilepsy on the human ALDH7A1 (Antiquitin-1) protein structure. a Ribbon structure of human ALDH7A1 with PDE-affected residues highlighted in red. Bound NAD+ cofactor shown in yellow. b Molecular surface depiction with accessible mutant residues highlighted in red. Residues surrounding the substrate binding pocket are highlighted in green. Bound NAD+ is again shown in yellow. Asterisks indicate that the residue is surface accessible but not visible on given structures either because they are found within a binding pocket (ASN167 and ALA171) or hidden behind other structural features (GLY255 and GLY263)

Gunter Scharer, et al. J Inherit Metab Dis. ;33(5):571-581.
3.
Fig. 1

Fig. 1. From: The genotypic and phenotypic spectrum of pyridoxine-dependent epilepsy due to mutations in ALDH7A1.

Overview of all mutations identified in ALDH7A1 (Antiquitin-1). All mutations identified from the literature (Mills et al. 2006; Plecko et al. 2007; Salomons et al. 2007; Kanno et al. 2007; Kluger et al. 2008; Kaczorowska et al. 2008; Striano et al 2009; Bennett et al. 2009; Gallagher et al. 2009; Schmitt et al. 2010; Millet et al. 2010) and in this study are shown. Mutations recurring more than twice are shown in red. Mutations are organized as missense, nonsense, or splice mutations and deletions or insertions. The splice-site mutations are IVS1+2T>G is c.108+2T>G; IVS2+1G>A is c.162+1G>A; IVS3+2T>A is c.228+2T>A; IVS5+5G>A is c.433+5G>A; IVS5-1G>C is c.434-1G>C; IVS6del-1-3 is c.567del-1-3; IVS9+3-+ 6delAAGT is c.787+3+6delAAGT; IVS12+1G>A is c.1009+1G> A; IVS16+5G>A is c.1405+5G>A (nomenclature according to www.hgvs.org/mutnomn). The large intron 2 is drawn at half size. The 5′ and 3′ noncoding regions are drawn in light color

Gunter Scharer, et al. J Inherit Metab Dis. ;33(5):571-581.
4.
Fig. 2

Fig. 2. From: The genotypic and phenotypic spectrum of pyridoxine-dependent epilepsy due to mutations in ALDH7A1.

Effect of I431F and P403L mutations on ALDH7A1 protein structure. The I431F (a) and P403L (b) mutants were created in silico using Accelrys Discovery Studio software. Loop refinement was then performed followed by residue optimization and free energy minimizations. The mutant (yellow) and wild type (white) structures are superimposed to highlight differences in secondary and tertiary structure. The I431F mutation resulted in loss of β-sheet secondary structure and buckling of a loop into the hydrophobic surface required for monomer dimerization (a). The loss of a bend in the peptide backbone as a result of the P403L mutation causes conformational changes that negatively affect cofactor binding (b) including loss of hydrogen bonding (right circle) and steric interference (left circle)

Gunter Scharer, et al. J Inherit Metab Dis. ;33(5):571-581.

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