Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptor

Wang, Qian and Lynch, Joseph W. (2011) Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptor. Journal of Biological Chemistry, 286 44: 38814-38824.


Author Wang, Qian
Lynch, Joseph W.
Title Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptor
Journal name Journal of Biological Chemistry  (ERA 2012 Listed)    (ERA 2010 Rank A*)   Check publisher's open access policy
Publication date 2011-11
Sub-type Article
DOI 10.1074/jbc.M111.273631
Volume number 286
Issue number 44
ISSN 0021-9258
1083-351X
Start page 38814
End page 38824
Total pages 20
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology, Inc.
Collection year 2012
Language eng
Formatted abstract Background:
Despite its physiological significance, the structural basis of desensitization in Cys-loop
receptors is unknown.

Results:
Fluorescent reporters attached to residues at the interface of the glycine receptor ligandbinding and transmembrane domains indicate that activation and desensitization induce distinct local conformational changes.

Conclusion:
Desensitization induces an interfacial conformational change incompatible with activation.

Significance:
This provides a mechanism for understanding desensitization.
Keyword Cys-loop receptor
Chloride channel
Voltage-clamp
Fluorescence
Neurotransmitter-gated
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes First Published on 14 September 2011.

 
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Created: Mon, 17 Oct 2011, 11:14:55 EST by Professor Joseph Lynch on behalf of Queensland Brain Institute