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

<table>Distribution of the amino acid residues involved in disease-causing mutations in the Cx50 homology model. Ribbon view of the Cx50 homology model is shown (constructed using the SWISS-MODEL server). Different regions of the protein are marked (N-terminal, TM-transmembrane domains, extracellular loops, cytoplasmic region, and C-terminal). Sixteen residues that are point-mutated to cause congenital cataract are indicated in the homology model (red spheres).</table>

BioMed Research International

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Figure 1: Structure-Function Correlation Analysis of Connexin50 Missense Mutations Causing Congenital Cataract: Electrostatic Potential Alteration Could Determine Intracellular Trafficking Fate of Mutants 

Figure 1 | Structure-Function Correlation Analysis of Connexin50 Missense Mutations Causing Congenital Cataract: Electrostatic Potential Alteration Could Determine Intracellular Trafficking Fate of Mutants 