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Glycoprotein‐binding site of dystrophin is confined to the cysteine‐rich domain and the first half of the carboxy‐terminal domain
Author(s) -
Suzuki Atsushi,
Yoshida Mikiharu,
Yamamoto Hideko,
Ozawa Eijiro
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81265-n
Subject(s) - dystrophin , duchenne muscular dystrophy , glycoprotein , domain (mathematical analysis) , terminal (telecommunication) , cysteine , binding domain , chemistry , utrophin , binding site , gene product , gene , biology , microbiology and biotechnology , genetics , biochemistry , gene expression , computer science , enzyme , mathematical analysis , telecommunications , mathematics
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 findings may provide it molecular basis of the disease.