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Comment
. 2000 Dec 5;97(25):13464-6.
doi: 10.1073/pnas.011510597.

The dystrophin-associated glycoprotein complex: what parts can you do without?

H L Sweeney  1 , E R Barton
Affiliations
Comment

The dystrophin-associated glycoprotein complex: what parts can you do without?

H L Sweeney et al. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Figure 1
Figure 1
Schematic representation of the dystrophin-associated glycoprotein complex. The N-terminal, actin-binding domain of dystrophin in purple is associated with the cortical actin. The C-terminal domain associates with β-dystroglycan and with α- and β-syntrophin and dystrobrevin. nNOS is known to interact with the syntrophins as well as with caveolin.
Figure 2
Figure 2
Domains of the dystrophin molecule. The N terminus contains the primary actin-binding site, whereas the C terminus contains the β-dystroglycan, dystrobrevin, and syntrophin-binding sites. The N- and C-terminal domains are connected by 24 spectrin-like repeats, some of which have been shown to bind actin (9). The four “hinge” regions are denoted H1–H4.
See this image and copyright information in PMC

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