Bioinformatics analysis of γD-crystallin protein P23T mutation in a congenital cataract family
A Pro-23→Thr (P23T) substitution in γD-crystallin protein was identified in a hereditary congenital cataract family through previous study. The amino acid sequence, protein domain and motifs, and three-dimension structure of γD-crystallin protein and its mutant were analyzed and predicted. The resul...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Zhejiang University Press
2004-01-01
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| Series: | 浙江大学学报. 农业与生命科学版 |
| Subjects: | |
| Online Access: | https://www.academax.com/doi/10.3785/1008-9209.2004.01.0109 |
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| Summary: | A Pro-23→Thr (P23T) substitution in γD-crystallin protein was identified in a hereditary congenital cataract family through previous study. The amino acid sequence, protein domain and motifs, and three-dimension structure of γD-crystallin protein and its mutant were analyzed and predicted. The results showed that the mutation of γD-crystallin protein could affect the ability of the protein to bind itself with calcium ions, thereby inducing dynamic unbalance of the calcium ions in lens. The inter-molecular hydrogen-bonds were rearranged, which would reduce the solubility of mutant γD protein. Protein modeling suggests that the effect of this mutation is a subtle one which affect the local polarity of the crystallin molecule surface, and may affect the manner of interaction between γD-crystallin protein and other proteins. |
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| ISSN: | 1008-9209 2097-5155 |