Computer construction and analysis of protein models of the mutant gammaD-crystallin gene / 中华医学杂志(英文版)
Chinese Medical Journal
;
(24): 738-741, 2005.
Artigo
em Inglês
| WPRIM
| ID: wpr-288343
ABSTRACT
<p><b>BACKGROUND</b>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.</p><p><b>METHODS</b>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.</p><p><b>RESULTS</b>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.</p><p><b>CONCLUSION</b>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.</p>
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Fisiologia
/
Simulação por Computador
/
Modelos Moleculares
/
Química
/
Estrutura Terciária de Proteína
/
Gama-Cristalinas
/
Genética
/
Ligação de Hidrogênio
/
Mutação
Tipo de estudo:
Estudo prognóstico
Limite:
Animais
Idioma:
Inglês
Revista:
Chinese Medical Journal
Ano de publicação:
2005
Tipo de documento:
Artigo
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