Conformational changes of type II regulatory subunit of cAMP‐ dependent protein kinase on cAMP binding

FEBS Letters

Johnson, Dennis R.¹  Wong, Shan S.¹ 

[1] The Biochemistry Program, Department of Chemistry, University of Lowell, Lowell, MA 01854, USA

关键词: cyclic AMP-dependent protein kinase;    cyclic AMP-binding protein;    Conformation;    CD;   

DOI  :  10.1016/0014-5793(89)81395-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of cAMP on the conformation of the regulatory subunit of type II cAMP-dependent protein kinase (RII) from bovine heart was investigated by UV-difference and circular dichroism (CD) spectroscopy. The UV-difference spectrum of RII with and without cAMP showed a positive band around 278 nm and a negative band at 256 nm. Similarly, cAMP enhanced the ellipticity of RII in the region between 280 and 300 nm and decreased that between 250 and 280 nm. In addition, cAMP transformed the far-UV CD spectrum of RII from that of a negative band minimally at 209 nm with a shoulder at 223 nm to one with two minima at 222 and 211 nm. These data show that cAMP induces conformational changes of RII upon binding. Such structural changes may be the basis of activation of cAMP-dependent protein kinases by cAMP.

【 授权许可】

Unknown