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FEBS Lett. 2014 Nov 3;588(21):3802-7. doi: 10.1016/j.febslet.2014.08.031. Epub 2014 Sep 12.

Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.

Author information

1
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences RAS, Str. Miklukho-Maklaya 16/10, Moscow 117997, Russian Federation. Electronic address: mineev@nmr.ru.
2
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences RAS, Str. Miklukho-Maklaya 16/10, Moscow 117997, Russian Federation; Lomonosov Moscow State University, Moscow 119991, Russian Federation.
3
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences RAS, Str. Miklukho-Maklaya 16/10, Moscow 117997, Russian Federation.

Abstract

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.

KEYWORDS:

Dimerization; Free energy; Spatial structure; Toll-like receptor; Transmembrane domain

PMID:
25217833
DOI:
10.1016/j.febslet.2014.08.031
[Indexed for MEDLINE]
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