Journal: Nature communications
Article Title: Cryo-EM structures of the membrane repair protein dysferlin.
doi: 10.1038/s41467-024-53773-6
Figure Lengend Snippet: Fig. 3 | Key interactions in the dysferlin monomer. a Two views (front, back) of the pentameric ring formed by the C2B, C2E, C2D, C2C, and composite C2 domain and stabilized by the C2D-C2E linker. Individual domains are color-coded. b Schematic representation of the pentameric ring. Color code according to panel a. c Residue-level interactions at interdomain interfaces in the pentameric ring. d Residue-level interactions of the FerI with the C2B, C2C, and C2E. Color code according to panel a. The electrostatic potential distribution is shown for the C2B, C2C, and C2E (left). e The C2E-C2F (grey) and C2F-C2G (grey) linkers connect the respective domains. The C2E insert interacts with the C2E (yellow), C2F (blue), and
Article Snippet: The codon-optimized dysferlin cDNA (Addgene plasmid # 67878, a gift from Matthew Hirsch)60 was amplified and inserted upstream of a coding sequence for a PreScission protease cleavage site and two strep II tags into a pFastBac1 vector via restriction-fee cloning.
Techniques: Residue