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

FEBS Lett. 1992 Aug 17;308(2):154-60. doi: 10.1016/0014-5793(92)81265-n.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Blotting, Western
  • Chromatography, Affinity
  • Cysteine / metabolism*
  • Dystrophin / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Glycoproteins / metabolism*
  • Molecular Sequence Data
  • Peptide Fragments / metabolism
  • Peptide Mapping
  • Rabbits

Substances

  • Dystrophin
  • Glycoproteins
  • Peptide Fragments
  • Cysteine