Figure 1From: Assessment of the structural and functional impact of in-frame mutations of the DMD gene, using the tools included in the eDystrophin online databaseThe dystrophin molecule and its partners. (A) Schematic representation of the molecule with the structural domains CH1 and CH2, constituting actin-binding domain 1, hinges 1 to 4 (H1 to H4), spectrin-like repeats 1 to 24 (R1 to R24); the WW domain and EF hand–region constituting the Cys-rich domain; ZZ, the zinc finger domain; and the C-terminal domain (C term) and its partners. (B) Model of the three-dimensional structure of repeat 7 folded into a triple coiled-coil, consisting of three helices, A, B, and C, joined by two loops, AB and BC. (C) Model of the three-dimensional structure of tandem repeats R7-8 of the rod domain. Each repeat is composed of three alpha helices folded into a triple coiled-coil: R7 (helices A, B, and C, joined by loops AB and BC) and R8 (helices A’, B’ and helix C’, joined by loops A’B’ and B’C’). A long common helical linker is formed between the two repeats by R7 helix C and R8 helix A’.Back to article page