Background γD-crystallin plays an important role in human cataract formation. Being highly stable, γD-crystallin proteins are composed of two domains. In this study we constructed and analyzed protein models of the...Background γD-crystallin plays an important role in human cataract formation. Being highly stable, γD-crystallin proteins are composed of two domains. In this study we constructed and analyzed protein models of the mutant γD-crystallin gene, which caused a special fasciculiform congenital cataract affecting a large Chinese family. Methods γD-crystallin protein structure was predicted by Swiss-Model software using bovine γD-crystallin as a template and Prospect software using human βb2-crystallin as a template. The models were observed with a Swiss-Pdb viewer.Results The mutant γD-crystallin structure predicted by the Swiss-Model software showed that proline23 was an exposed surface residue and P23T change made a decreased hydrogen bond distance between threonine23 and asparagine49. The mutant γD-crystallin structure predicted by the Prospect software showed that the P23T change exerted a significant effect on the protein’s tertiary structure and yielded hydrogen bonds with aspartic acid21, asparagine24, asparagine49 and serine74.Conclusion The mutant γD-crystallin gene has a significant effect on the protein’s tertiary structure, supporting that alteration of γ-crystallin plays an important role in human cataract formation.展开更多
文摘Background γD-crystallin plays an important role in human cataract formation. Being highly stable, γD-crystallin proteins are composed of two domains. In this study we constructed and analyzed protein models of the mutant γD-crystallin gene, which caused a special fasciculiform congenital cataract affecting a large Chinese family. Methods γD-crystallin protein structure was predicted by Swiss-Model software using bovine γD-crystallin as a template and Prospect software using human βb2-crystallin as a template. The models were observed with a Swiss-Pdb viewer.Results The mutant γD-crystallin structure predicted by the Swiss-Model software showed that proline23 was an exposed surface residue and P23T change made a decreased hydrogen bond distance between threonine23 and asparagine49. The mutant γD-crystallin structure predicted by the Prospect software showed that the P23T change exerted a significant effect on the protein’s tertiary structure and yielded hydrogen bonds with aspartic acid21, asparagine24, asparagine49 and serine74.Conclusion The mutant γD-crystallin gene has a significant effect on the protein’s tertiary structure, supporting that alteration of γ-crystallin plays an important role in human cataract formation.
