Literature DB >> 25217833

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

Konstantin S Mineev1, Sergey A Goncharuk2, Alexander S Arseniev3.   

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.
Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Entities:  

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

Mesh：

Substances：

Year:  2014        PMID： 25217833     DOI： 10.1016/j.febslet.2014.08.031

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  10 in total

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Authors:  D M Lesovoy; K S Mineev; P E Bragin; O V Bocharova; E V Bocharov; A S Arseniev
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Authors:  Vladislav A Lushpa; Marina V Goncharuk; Cong Lin; Arthur O Zalevsky; Irina A Talyzina; Aleksandra P Luginina; Daniil D Vakhrameev; Mikhail B Shevtsov; Sergey A Goncharuk; Alexander S Arseniev; Valentin I Borshchevskiy; Xiaohui Wang; Konstantin S Mineev
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  10 in total

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