Fig. 2: NAA60 protein sequence and structural features predict functional implications of NAA60 variants. | Nature Communications

Fig. 2: NAA60 protein sequence and structural features predict functional implications of NAA60 variants.

From: Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications

Fig. 2

a Alignment of the NAA60 amino acids corresponding to the GNAT fold across different species shows strong conservation of the regions affected by NAA60 variants found in PFBC cases of the seven families (Family 1–7). UNIPROT accession numbers: human, Q9H7X0; D. rerio (DANRE), A3KPA3; bovine (BOVIN), Q17QK9; mouse, Q9DBU2; rat, Q3MC1; D. melanogaster (DROME), Q95SX8. b Structure of wild-type NAA60 (PDB: 5ICV, amino acids 4–184 https://www.rcsb.org/structure/5icv) shown in gray from three different angles with the bound CoA-Ac-MKAV bisubstrate analog in stick representation. c PDB structure modified in PyMol to visualize the truncated proteins predicted from the PFBC NAA60 variants F1 and F2/3. The Ac-CoA motif is indicated in yellow. d PDB structure modified in PyMol to visualize the PFBC NAA60 missense variants in F4-F7. e Interaction figures derived from DynaMut predictions displaying interaction forces between the mutated residues in F4-F7 and surrounding residues.

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