The interaction of actin with 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 nuclear magnetic resonance;    Dystrophin;    F-actin;    Interaction;    α-Actinin;    Synthetic peptide;   

DOI  :  10.1016/0014-5793(90)80728-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Proton NMR spectroscopy of synthetic peptides corresponding to defined regions of human dystrophin has been employed to study the interaction with F-actin. No evidence of interaction with a C-terminal region corresponding to amino acid residues 3429–3440 was obtained. F-actin restricted the mobility of residues 19–27 in a synthetic peptide corresponding to residues 10–32. This suggests that this is a site of F-actin interaction in the intact dystrophin molecule. Identical sequences to that of residues 19—22 in dystrophin, namely Lys-Thr-Phe-Thr are also present in the N-terminal regions of the α-actinins implying this is also a site of F-actin interaction with α-actinin.

【 授权许可】

Unknown