Utrophin ABD binds to F-actin in an open conformation

作者：Broderick Mike J F; Bobkov Andrey; Winder Steve J^*

来源：FEBS Open Bio, 2012, 2: 6-11.

DOI：10.1016/j.fob.2012.01.001

• alpha-Actinin
• Actin binding domain
• Calponin homology domain
• Differential scanning calorimetry
• Dystrophin
• Spectrin

Structural analyses of actin binding regions comprising tandem calponin homology domains alone and when bound to F-actin have revealed a number of different conformations with calponin homology domains in %26apos;open%26apos; and %26apos;closed%26apos; positions. In an attempt to resolve these issues we have examined the properties of the utrophin actin binding domain in open and closed conformations in order to verify the conformation when bound to F-actin. Locking the actin binding domain in a closed conformation using engineered cysteine residues in each calponin homology domain reduced the affinity for F-actin without affecting the stoichiometry furthermore differential scanning calorimetry experiments revealed a reduction in melting temperature on binding to actin. The data suggest the amino-terminal utrophin actin binding domain is in an open conformation in solution and when bound to F-actin.

• 出版日期2012
• 单位河北医科大学