"Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors.
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.
Kim
S H
SH
Department of Chemistry, University of California, Berkeley 94720.
D001419:Bacteria / Q000737:chemistry*; D003460:Crystallization; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation; D017459:Receptors, Amino Acid / Q000737:chemistry*; D015398:Signal Transduction
D046911:Macromolecular Substances; D017459:Receptors, Amino Acid; C031959:aspartic acid receptor