Preliminary study of the spatial structural and functional changes of dystrophin after exon-3 deletion / 南方医科大学学报
Journal of Southern Medical University
; (12): 938-941, 2008.
Article
en Zh
| WPRIM
| ID: wpr-280064
Biblioteca responsable:
WPRO
ABSTRACT
<p><b>OBJECTIVE</b>To explore the structural and functional changes of dystrophin molecule after exon 3 deletion.</p><p><b>METHODS</b>Three-dimensional models of dystrophin comprising the major domains were established before and after exon 3 deletion using SWISS-MODEL server. The motifs and structural domains of dystrophin after exon 3 deletion were searched in Pfam database, and the crystal structure of the actin-binding domain in the dystrophin molecule was analyzed using Rasmol software.</p><p><b>RESULTS</b>Torsion of the N-terminal actin-binding domain occurred in the dystrophin molecule after deletion of exon 3. Homology analysis based on Pfam database searches indicated that following exon 3 deletion, the Bit score of the first calponin homology (CH1) domain was decreased from 108 to 36.5 while its expectation value increased from 2.3e-9 to 8.1e-8. The deletion also resulted in the absence of the spiral region C from the CH1 domain.</p><p><b>CONCLUSION</b>Exon 3 deletion in the dystrophin-coding sequence decreases the stability of CH1 domain and prevents the formation of the junction interface where dystrophin binds to actin. The bioinformatics approach provides a new alternative for investigation of the pathogenesis of DMD pathogenesy investigation.</p>
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Unión Proteica
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Conformación Proteica
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Relación Estructura-Actividad
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Modelos Moleculares
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Química
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Exones
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Distrofina
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Eliminación de Secuencia
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Estructura Terciaria de Proteína
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Distrofia Muscular de Duchenne
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
Zh
Revista:
Journal of Southern Medical University
Año:
2008
Tipo del documento:
Article