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Fig. 3 | BMC Medical Genomics

Fig. 3

From: Whole exome sequencing revealed variants in four genes underlying X-linked intellectual disability in four Iranian families: novel deleterious variants and clinical features with the review of literature

Fig. 3

The 3-D structure of the ZDHHC9, GLRA2, and ATP2B3 proteins. A: The modeled structure of the mutated ZDHHC9 protein containing the p.Leu189Pro variant, the Leucine residue has been substituted with proline 189 (B, C); due to its irregular geometry, the proline residue destabilizes α-helices and probably disrupts the protein function. D: It illustrated the structure of the GLRA2 protein. Figure E shows that arginine 350 forms a salt bridge and a hydrogen bond with glutamic acid 347 and a salt bridge with arginine 343 (p.Arg350Cys). As a result of cysteine substitution, all of the mentioned hydrogen bonds are lost (F). G: The modeled structure of the ATP2B3 protein containing the p.Asp847Glu variant, the aspartic acid residue, has been substituted with glutamic acid 847 (H, I). As with aspartic acid, glutamic acid is an acidic residue; however, it has a smaller side chain, and due to its distance from the arginine 911 side chain, the salt bridge is broken

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BMC Medical Genomics

ISSN: 1755-8794

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