Published: 25 July, 2017 | Volume 1 - Issue 1 | Pages: 019-036
Figure 2:
Dystrophin complex. A) Dystrophin contains an N-terminus (NT), a filament-shaped central part, a cysteine-rich (CR) domain and a C-terminal (CT). The central part is composed of 24 Spectrin-Like Repeats (SLRs) numbered from 1 to 24 and four junction regions called Hinge numbered H1 to H4. There are two actin binding sites, one of which is located at the NT end and the other at the SLR11-15. SLR1-3 interact with the cell membrane and SLR 16 and 17 with neuronal Nitric Oxide Synthetase (nNOS). Dystrophin also interacts with microtubules at SLR20-23. A portion of H4 and the CR domain bind with the beta-dystroglycan (βDG) protein. CT interacts with syntrophin (Syn) and dystrobrevin (Dbr). Dystrophin complex allows the binding of cytoskeletal proteins (actin and microtubules) with laminin in the extracellular matrix (arrow). Sarcoglycans and sarcospan do not interact directly with dystrophin. However, they stabilize the dystrophin complex. The spectral type repeat α-helices. Image modified from [48]. B) Dystrophin comprises 24 SLRs. Each SLR is formed by 3 alpha helices (helixes A, B and C). The N-terminus (N-ter) is at the beginning of helix A and the C-terminus (C-ter) is at the end of helix C. The helix A is bonded to helix B by loop AB while the helix B is connected to helix C loop BC. Image modified from [49].
Read Full Article HTML DOI: 10.29328/journal.jgmgt.1001003 Cite this Article Read Full Article PDF
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