Figure 1. Genomic organization of the DMD gene locus to show promoter locations according to exon number, and size of translated products. B: brain, M: skeletal muscle, P: Purkinje cells, R: retinal, B3: brain-3, S: Schwann cell, G: general. The numbers following the term Dp represent the size of the dystrophin molecule generated in kilodaltons. (From Newey S (2000) Functional analysis of alpha dystrobrevin in muscle, DPhil thesis, University of Oxford, with permission.)

Figure 2. Schematic diagram of dystrophin showing protein interactions and localization in vivo at the muscle sarcolemma (-DG: -dystroglycan). The inclusion of four syntrophin molecules (syn) reflects the repeated -helical binding sites recognized in both dystrophin and dystrobrevin. However, the exact stoichiometry is not yet known for how many syntrophin molecules bind to this region. The specific isoforms of syntrophin and the associated signaling molecules that may be present are not fully elucidated. (Adapted from Burton E (1999) Investigation into the transcriptional regulation of utrophin: possible application in the therapy of Duchenne muscular dystrophy, DPhil thesis, University of Oxford and Newey S (2000) Functional analysis of alpha dystrobrevin in muscle, DPhil thesis, University of Oxford, with permission.)

Figure 3. Structural similarity between dystrophin isoforms and related proteins. H refers to the hinge region, CR refers to the cysteine-rich region, CT refers to the C-terminal region. - and -spectrin, and -actinin are shown as in vivo, as antiparallel dimers. Domains shown in black represent unique N-termini. (Adapted from Newey S (2000) DPhil thesis, University of Oxford, with permission.)