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“Frozen” dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors
Author(s) -
Kim SungHou
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560030201
Subject(s) - dimer , chemotaxis , transmembrane protein , biophysics , transmembrane domain , receptor , ligand (biochemistry) , cytoplasm , chemistry , signal transduction , microbiology and biotechnology , biochemistry , biology , organic chemistry
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.