Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures.

@article{Chi1997ApoSO,
  title={Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures.},
  author={Yonggui Chi and Hisao A Yokota and Sun Ran Kim},
  journal={FEBS letters},
  year={1997},
  volume={414 2},
  pages={327-32}
}
The aspartate receptor from E. coli is a dimeric transmembrane-signaling protein that mediates chemotaxis behavior and is the most studied system among the chemotaxis receptors to understand the molecular mechanism for transmembrane signaling. However, there is an unresolved issue for the structural event which initiates the transmembrane signal upon binding to the ligand. Biochemical and genetic evidence implies an intrasubunit mechanism (monomeric model) whereas crystallographic evidence… CONTINUE READING

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