Fig. 2

Diagrams of structural models for MAMLD1 (A). Amino-acid residue (dots): p.Pro334Ser is blue,p.Ala421Pro is light gray, p.Pro542Ser is light orange, p.Ser662Arg is light golden, p.Arg927Leu is pink, and p.Thr992Ile is white. Hydrogen bonding by MAMLD1 residues inthe wild type p.Pro359(B-1) and the mutated p.Pro359Ser(B-2) are shown in sticks format with difference signed by red arrows. Hydrogen bonding by MAMLD1 residues inthe wild type p.Pro542(C-1) and the mutated p.Pro542Ser(C-2) are shown in sticks format with difference signed by red arrows. In the visualisation of the predicted molecular surface, detail of the protein surface in the wild type p.Pro542(C-3) and the mutated p.Pro542Ser(C-4) are coloured by CPK notation (red, oxygen; blue, nitrogen; yellow, sulphur; grey, carbon) with distinction signed by light blue arrows and yellow circles. Hydrogen bonding by MAMLD1 residues inthe wild type p.Ser662(D-1) and the mutated p.Ser662Arg(D-2) are shown in sticks format with difference signed by red arrows. Detail of the protein surface in the wild type p.Ser662(D-3) and the mutated p.Ser662Arg(D-4) are coloured by CPK notation with distinction signed by light blue arrows and yellow circles. Hydrogen bonding by MAMLD1 residues inthe wild type p.Arg927(E-1) and the mutated p.Arg927Leu(E-2) are shown in sticks format with difference signed by red arrows. Detail of the protein surface in the wild type p.Arg927(E-3) and the mutated p.Arg927Leu(E-4) are coloured by CPK notation with distinction signed by light blue arrows and yellow circles