Fig. 2
From: MAN2A2-related glycosylation defects in autism and cognitive delay
Structural prediction analysis of wild-type and Arg560Gln-mutated MAN2A2 proteins. (a) Graphical representation of the wild-type MAN2A2 protein. (b) Graphical representation of the Arg560Gln-mutated MAN2A2 protein. In both the Figures the panel highlights different functional domains and regions using distinct colors: blue for extra domain regions, orange for the N-terminal catalytic domain of Golgi alpha-mannosidase IIx (residues 165–508), green for the Alpha-mannosidase middle domain (502–605), and red for the Glycosyl hydrolases family 38 C-terminal domain (765–970). N-linked glycosylation sites are marked with pink squares, while the nucleophile site Asn95 is indicated by a dark gray circle. (c) Close-up view of the wild-type Arg560 residue (cyan), showing seven hydrogen bonds: three with Glu529, one with Gly564, one with Leu556, and one with Thr1059. (d) Close-up view of the mutated Gln560 residue (cyan), forming three hydrogen bonds with Glu529, Gly564, and Leu556. (e) Graphical representation of hydrogen bonds within the Alpha-mannosidase middle domain (502–605) in the wild-type protein. (f) Graphical representation of hydrogen bonds within the Alpha-mannosidase middle domain (502–605) in the Arg560Gln-mutated protein.
