Chinese medical journal · 2005
Computer construction and analysis of protein models of the mutant gammaD-crystallin gene.
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Yao Ke, Sun Zhao-hui, Shentu Xing-chao, Wang Kai-jun, Tan Jian
Аннотация
BACKGROUND: Gammad-crystallin plays an important role in human cataract formation. Being highly stable, gammaD-crystallin proteins are composed of two domains. In this study we constructed and analyzed protein models of the mutant gammaD-crystallin gene, which caused a special fasciculiform congenital cataract affecting a large Chinese family.
METHODS: gammaD-crystallin protein structure was predicted by Swiss-Model software using bovine gammaD-crystallin as a template and Prospect software using human betab2-crystallin as a template. The models were observed with a Swiss-Pdb viewer.
RESULTS: The mutant gammaD-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 gammaD-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 gammaD-crystallin gene has a significant effect on the protein's tertiary structure, supporting that alteration of gamma-crystallin plays an important role in human cataract formation.
METHODS: gammaD-crystallin protein structure was predicted by Swiss-Model software using bovine gammaD-crystallin as a template and Prospect software using human betab2-crystallin as a template. The models were observed with a Swiss-Pdb viewer.
RESULTS: The mutant gammaD-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 gammaD-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 gammaD-crystallin gene has a significant effect on the protein's tertiary structure, supporting that alteration of gamma-crystallin plays an important role in human cataract formation.