Characterization of the calcyclin (S100A6) binding site of annexin XI‐A by site‐directed mutagenesis

FEBS Letters

Hidaka, Hiroyoshi¹  Sudo, Toshiki¹ 

[1]Department of Pharmacology, Nagoya University School of Medicine, Showa-ku, Nagoya 466-8550, Japan

关键词: Annexin XI;    Calcyclin;    S100A6;    Hydrophobic interaction;   

DOI  :  10.1016/S0014-5793(99)00014-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Residues in annexin XI-A essential for binding of calcyclin (S100A6) were examined by site-directed mutagenesis. GST fusion proteins with the calcyclin binding site of annexin XI-A, GST-AXI 34–62 and GST-AXI 49–77 bound to calcyclin-Sepharose Ca²⁺-dependently. The mutants GST-AXI L52E, M55E, A56E and M59E lost the binding ability, whereas GST-AXI A57E retained the ability. These results demonstrate that the hydrophobic residues L52, M55, A56 and M59 on one side surface of the α-helix are critical for the binding. Assays with GST fusion proteins and synthesized peptides corresponding to the calcyclin binding site indicated that other regions around the calcyclin binding site are important to stabilize the conformation.

【 授权许可】

Unknown