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Updated: Jul 4, 2026
Characterizing Exon Skipping Efficiency in DMD Patient Samples in Clinical Trials of Antisense Oligonucleotides
Published on: May 7, 2020
[Preliminary study of the spatial structural and functional changes of dystrophin after exon-3 deletion]
Ying-Yin Liang1, Cheng Zhang, Song-Lin Chen
1Department of Neurology, First Affiliated Hospital, Sun Yat-sen University, Guangzhou 510700, China.
Objective:
To explore the structural and functional changes of dystrophin molecule after exon 3 deletion.
Methods:
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.
Results:
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.
Conclusion:
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.
