Increase in the molecular weight and radius of gyration of apocalmodulin induced by binding of target peptide: evidence for complex formation

FEBS Letters

Yoshino, Hidenori²  Jinbo, Yuji¹  Izumi, Yoshinobu¹  Kuwamoto, Shigeo¹ 

[1] Graduate Program of Human Sensing and Functional Sensor Engineering, Graduate School of Science and Engineering, Yamagata University, 4-3-16 Jo-nan, Yonezawa 992-8510, Japan;Department of Chemistry, Sapporo Medical University, S-1, W-17, Chuo-ku, Sapporo 060-0061, Japan

关键词: Apocalmodulin;    Ca2+/calmodulin-dependent protein kinase IV calmodulin target site;    Small-angle X-ray scattering;    Complex state;    Linker flexibility;    Electrostatic interaction;   

DOI  :  10.1016/S0014-5793(01)02375-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Small-angle X-ray scattering was used to investigate a complex state of apocalmodulin induced by the binding of a Ca²⁺/calmodulin-dependent protein kinase IV calmodulin target site. Upon binding of the peptide, the molecular weight for apocalmodulin increased by 8.4%, which provides direct evidence for the formation of a calmodulin/target peptide complex. Comparison of the radius of gyration and Kratky plots of the apocalmodulin/peptide complex with those of apocalmodulin indicates that the overall conformation remains unchanged but the flexibility of the central linker decreases. An analysis of residue pairs between calmodulin and the target peptides suggests that the complex formation is induced by electrostatic interactions and subsequent van der Waals interactions.

【 授权许可】

Unknown