Sequence analysis suggests the presence of an IG-like domain in the N-terminal region of α-dystroglycan which was crystallized after mutation of a protease susceptible site (Arg 168 → His)
Recently, we demonstrated that the N-terminal region of mouse α-dystroglycan represents an autonomously folding globular domain, organized into at least two subdomains (Brancaccio et al., Eur. J. Biochem. 246, 166–172, 1997). We have now found a similarity between a part of the α-dystroglycan N-term...
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Veröffentlicht in: | Matrix biology 1998-11, Vol.17 (7), p.495-500 |
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