Related Experiment Video
Updated: Aug 18, 2026

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
Published on: October 13, 2022
Computer construction and analysis of protein models of the mutant gammaD-crystallin gene
Ke Yao1, Zhao-hui Sun, Xing-chao Shentu
1Eye Center, Affiliated Second Hospital, Zhejiang University School of Medicine, Hangzhou 310009, China. xlren@zju.edu.cn
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.
More Related Videos
05:48Removal of an Internal Translational Start Site from mRNA While Retaining Expression of the Full-Length Protein
Published on: March 16, 2022
09:19Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization
Published on: March 16, 2020