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"Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors.

Authors
Journal
Protein Science
0961-8368
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Keywords
  • Research Article

Abstract

The crystal structures of the ligand binding domain of a bacterial aspartate receptor suggest a simple mechanism for transmembrane signaling by the dimer of the receptor. On ligand binding, one domain rotates with respect to the other, and this rotational motion is proposed to be transmitted through the membrane to the cytoplasmic domains of the receptor.

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