Deletion analysis of the dystrophin‐actin binding domain

FEBS Letters

Corrado, K.¹  Chamberlain, J.S.¹  Mills, P.L.¹ 

[1] Department of Human Genetics, University of Michigan, Ann Arbor, MI 48109-0618, USA

关键词: Dystrophin;    Actin binding site;    Duchenne muscular dystrophy;    α-Actinin;   

DOI  :  10.1016/0014-5793(94)00397-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three sequence motifs at the N-terminus of dystrophin have previously been proposed to be important for binding to actin. By analyzing a series of purified bacterial fusion proteins deleted for each of these sites we have demonstrated that none of the three are critical for dystrophin-actin interactions. Instead, our data suggest that sequences in the N-terminal 90 amino acids of dystrophin, excluding a conserved KTFT motif, contain the major site for interaction with actin.

【 授权许可】

Unknown