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Toll‐like receptor 3 transmembrane domain is able to perform various homotypic interactions: An NMR structural study
Author(s) -
Mineev Konstantin S.,
Goncharuk Sergey A.,
Arseniev Alexander S.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.08.031
Subject(s) - transmembrane domain , transmembrane protein , helix (gastropod) , nuclear magnetic resonance spectroscopy , chemistry , toll like receptor , innate immune system , receptor , tlr3 , domain (mathematical analysis) , biophysics , microbiology and biotechnology , biology , stereochemistry , biochemistry , mathematics , ecology , mathematical analysis , snail
Toll‐like receptors (TLRs) take part in both the innate and adaptive immune systems. The role of the transmembrane domain in TLR signaling is still elusive, while its importance for the TLR activation was clearly demonstrated. In the present study the ability of the TLR3 transmembrane domain to form dimers and trimers in detergent micelles was shown by solution NMR spectroscopy. Spatial structures and free energy magnitudes were determined for the TLR3 transmembrane domain in dimeric and trimeric states, and two possible surfaces that may be used for the helix–helix interaction by the full‐length TLR3 were revealed.