Skip to main content
. 2019 Jul 17;10:3134. doi: 10.1038/s41467-019-10966-8

Fig. 2.

Fig. 2

Mapping of the most common mutations on to the OPCML crystal structure homodimer. The OPCML homodimer is shown in space-filling representation with one monomer in white and the other wheat. Mutations associated with the wheat monomer are underlined. Mutations in domains 1 and 3 are drawn on the outside of the dimer, whilst domain 2 associated mutations are shown on the inside. The most commonly mutated sites (sites mutated 8 or 9 times) are shown in blue with the residue name in bold. Residues mutated 4, 5 or 6 times are shown in marine and residues mutated 3 times shown in sky blue. For simplicity, mutations found 1 or 2 times are not highlighted, with the exception of K230