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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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 |
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Online Access: | https://www.academax.com/doi/10.3785/1008-9209.2004.01.0109 |
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author | DONG Qi ZHENG Shu XU Wei-zhen CAI Shan-rong YAO Ke |
author_facet | DONG Qi ZHENG Shu XU Wei-zhen CAI Shan-rong YAO Ke |
author_sort | DONG Qi |
collection | DOAJ |
description | 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. |
format | Article |
id | doaj-art-c3b83d5197b24567b6df85f6e93c276f |
institution | Matheson Library |
issn | 1008-9209 2097-5155 |
language | English |
publishDate | 2004-01-01 |
publisher | Zhejiang University Press |
record_format | Article |
series | 浙江大学学报. 农业与生命科学版 |
spelling | doaj-art-c3b83d5197b24567b6df85f6e93c276f2025-08-01T05:38:32ZengZhejiang University Press浙江大学学报. 农业与生命科学版1008-92092097-51552004-01-013010911310.3785/1008-9209.2004.01.010910089209Bioinformatics analysis of γD-crystallin protein P23T mutation in a congenital cataract familyDONG QiZHENG ShuXU Wei-zhenCAI Shan-rongYAO KeA 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.https://www.academax.com/doi/10.3785/1008-9209.2004.01.0109congenital cataract familyγD-crystallin proteinmutationbioinformatics |
spellingShingle | DONG Qi ZHENG Shu XU Wei-zhen CAI Shan-rong YAO Ke Bioinformatics analysis of γD-crystallin protein P23T mutation in a congenital cataract family 浙江大学学报. 农业与生命科学版 congenital cataract family γD-crystallin protein mutation bioinformatics |
title | Bioinformatics analysis of γD-crystallin protein P23T mutation in a congenital cataract family |
title_full | Bioinformatics analysis of γD-crystallin protein P23T mutation in a congenital cataract family |
title_fullStr | Bioinformatics analysis of γD-crystallin protein P23T mutation in a congenital cataract family |
title_full_unstemmed | Bioinformatics analysis of γD-crystallin protein P23T mutation in a congenital cataract family |
title_short | Bioinformatics analysis of γD-crystallin protein P23T mutation in a congenital cataract family |
title_sort | bioinformatics analysis of γd crystallin protein p23t mutation in a congenital cataract family |
topic | congenital cataract family γD-crystallin protein mutation bioinformatics |
url | https://www.academax.com/doi/10.3785/1008-9209.2004.01.0109 |
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