Conformational change in the vinculin C-terminal depends on a critical histidine residue (His-906).

@article{Miller2001ConformationalCI,
  title={Conformational change in the vinculin C-terminal depends on a critical histidine residue (His-906).},
  author={Gregory J. Miller and E. Hazel Ball},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 31},
  pages={28829-34}
}
A phospholipid-controlled interaction between the N-terminal and C-terminal domains of vinculin is thought to be a major mechanism that regulates binding activities of the protein. To probe the mechanisms underlying these interactions we used chemical modification and site-directed mutagenesis directed at histidine residues. Diethylpyrocarbonate (DEPC) modification of the C-terminal, but not the N-terminal, domain greatly decreased affinity of the N-terminal-C-terminal binding, implicating… CONTINUE READING