Conformational dynamics underlie the activity of the auxin-binding protein, Nt-abp1.

@article{David2001ConformationalDU,
  title={Conformational dynamics underlie the activity of the auxin-binding protein, Nt-abp1.},
  author={Karine Myriam David and Eug{\'e}nie Carnero-Diaz and Nathalie Leblanc and Mich{\`e}le Monestiez and Jeanne Grosclaude and Catherine Perrot-Rechenmann},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 37},
  pages={34517-23}
}
The auxin-binding protein 1 (ABP1) has been proposed to be involved in the perception of the phytohormone at the plasma membrane. Site-directed mutagenesis was performed on highly conserved residues at the C terminus of ABP1 to investigate their relative importance in protein folding and activation of a functional response at the plasma membrane. Detailed analysis of the dynamic interaction of the wild-type ABP1 and mutated proteins with three distinct monoclonal antibodies recognizing… CONTINUE READING

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