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Protein Science, Vol 3, Issue 2 159-165, Copyright © 1994 by Cold Spring Harbor Laboratory Press

REVIEWS

``Frozen'' dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors

S. H. KIM
Department of Chemistry and Lawrence Berkeley Laboratory, University of California, Berkeley, California 94720

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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