Figure 3 | European Journal of Human Genetics

Figure 3

From: De novo missense mutations in the NAA10 gene cause severe non-syndromic developmental delay in males and females

Figure 3

Structural effects of the p.(Val107Phe) and p.(Arg116Trp) variants in the acetyltransferase domain of Naa10 (cyan ribbon). The cofactor coenzyme A (CoA) is shown in space-filled presentation and coloured according to the atom type. The variant site is shown in green and key interacting residues in magenta. (a) Val107 is located in the hydrophobic core of the enzyme and tightly interacts with other hydrophobic residues, such as Met98. (b) Phe107 cannot be accommodated in the hydrophobic core due to its larger side chain and forms steric clashes with adjacent residues (denoted by a red arrow). These clashes are expected to cause protein unfolding and loss of enzymatic activity. (c) Arg116 is located close to the cofactor coenzyme A (CoA). (d) Trp116 preferentially adopts a side chain orientation that interferes with CoA binding. The steric clashes between Trp116 and CoA are indicated by a red arrow. These clashes are expected to hamper CoA binding and to reduce the enzymatic activity.

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