Glycoprotein‐binding site of dystrophin is confined to the cysteine‐rich domain and the first half of the carboxy‐terminal domain

FEBS Letters

Ozawa, Eijiro¹  Yoshida, Mikiharu¹  Suzuki, Atsushi¹  Yamamoto, Hideko¹ 

[1] Division of Cell Biology, National Institute of Neuroscience, NCNP, 4-1-1 Ogawa-Higashi, Kodaira, Tokyo 187, Japan

关键词: Dystrophin;    Sarcolemma;    Glycoprotein-binding site;    Calpain;    Peptide mapping;    DAPC;    dystrophin and its associated protein complex;    WGA;    wheat germ agglutinin;   

DOI  :  10.1016/0014-5793(92)81265-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown