Send to

Choose Destination
J Mol Biol. 1994 Jan 28;235(4):1271-7.

conformation and phasing of dystrophin structural repeats.

Author information

Medical Research Council Muscle and Cell Motility Unit, King's College, London.


The presumptive rod domain of dystrophin contains a series of degenerate repeating sequences with homology to those of spectrin. To determine the relation of the implied structural repeating units to the sequence repeat (the phasing), recombinant fragments of the domain of dystrophin were prepared by expression in Escherichia coli. The phasing was established by identifying the minimum sequence element that would form a stable fold of high (approx. 75%) alpha-helicity: by contrast, incorrectly phased fragments had labile structure with an average alpha-helicity of about 40%. The isolated folded structural repeat showed high stability towards proteolysis and a urea-denaturation profile with a plateau at low denaturant concentration, indicative of a unique folded conformation. The phasing is consistent with a structure inferred from analysis of the amino acid sequence and also found in spectrin, in which each structural repeat comprises a three-stranded coiled-coil, made up of one short helix (approx. 30 residues) and the N and C-terminal halves of two separate long helices, such that each long helix participates in the formation of two contiguous structural units.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center