Structure-Function Correlation Analysis of Connexin50 Missense Mutations Causing Congenital Cataract: Electrostatic Potential Alteration Could Determine Intracellular Trafficking Fate of Mutants

Figure 2

Three-dimensional location of the functionally characterized Cx50 mutations in the homology model of the wild-type protein. Ribbon view of the Cx50 homology model is shown. Ten residues involved with 11 missense changes are represented as spheres colored according to solvent accessibility (using the Swiss-PdbViewer—blue through red corresponding to buried-through-exposed residues; see color bar). Seven mutations (R23T, V44E, W45S, D47N, E48K, and P88S/Q) with loss of gap junction conductance involved 6 structurally buried residues (blue spheres). Other 2 mutation-involving residues are relatively exposed (G46 and R198 [equivalent to mouse R205]) (green spheres). E201 (blue sphere) represents the mistrafficked mutant E201K (gap junctional conductance has not been reported yet).