Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxy-terminal domain.
Dystrophin, a protein product of the Duchenne muscular dystrophy gene, is thought to associate with the muscle membrane by way of a glycoprotein complex which was co-purified with dystrophin. Here, we firstly demonstrate direct biochemical evidence for association of the carboxy-terminal region of dystrophin with the glycoprotein complex. The binding site is found to lie further inward than previously expected and confined to the cysteine-rich domain and the first half of the carboxy-terminal domain. Since this portion corresponds well to the region that, when missing, results in severe phenotypes, our finding may provide a molecular basis of the disease.
Suzuki
A
A
Division of Cell Biology, NCNP, Tokyo, Japan.
Yoshida
M
M
Yamamoto
H
H
Ozawa
E
E
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D015153:Blotting, Western; D002846:Chromatography, Affinity; D003545:Cysteine / Q000378:metabolism*; D016189:Dystrophin / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D010449:Peptide Mapping; D011817:Rabbits
D016189:Dystrophin; D006023:Glycoproteins; D010446:Peptide Fragments; D003545:Cysteine