Binding sites involved in the interaction of actin with the N‐terminal region of dystrophin

FEBS Letters

Levine, B.A.²  Moir, A.J.G.¹  Perry, S.V.³  Patchell, V.B.³ 

[1] Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK;Department of Inorganic Chemistry, University of Oxford, Oxford, UK;Department of Physiology, University of Birmingham, Birmingham, UK

关键词: Proton NMR;    Dystrophin;    F-actin;    Interaction;    α-Actinin;    β-Spectrin;   

DOI  :  10.1016/0014-5793(92)80019-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two actin-binding sites have been identified on human dystrophin by proton NMR spectroscopy of synthetic peptides corresponding to defined regions of the polypeptide sequence. These are Actin-Binding Site 1 (ABS1) located at residues 17–26 and Actin-Binding Site 2 (ABS2) in the region of residues 128–156. Using defined fragments of the actin amino acid sequence, ABS1 has been shown to bind to actin in the region represented by residues 83–117 and ABS2 to the C-terminal region represented by residues 350–375. These dystrophin-binding sites lie on the exposed domain in the actin filament.

【 授权许可】

Unknown