Toll‐like receptor 3 transmembrane domain is able to perform various homotypic interactions: An NMR structural study. Issue 21 (12th September 2014)
- Record Type:
- Journal Article
- Title:
- Toll‐like receptor 3 transmembrane domain is able to perform various homotypic interactions: An NMR structural study. Issue 21 (12th September 2014)
- Main Title:
- Toll‐like receptor 3 transmembrane domain is able to perform various homotypic interactions: An NMR structural study
- Authors:
- Mineev, Konstantin S.
Goncharuk, Sergey A.
Arseniev, Alexander S. - Abstract:
- 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. Abstract : We study structure and oligomerization equilibrium of TLR3 transmembrane domain in micelles. TLR3 transmembrane domain forms both dimers and trimers. Spatial structures of dimers and trimers were determined. The standard free energy of dimerization and trimerization was measured.
- Is Part Of:
- FEBS letters. Volume 588:Issue 21(2014)
- Journal:
- FEBS letters
- Issue:
- Volume 588:Issue 21(2014)
- Issue Display:
- Volume 588, Issue 21 (2014)
- Year:
- 2014
- Volume:
- 588
- Issue:
- 21
- Issue Sort Value:
- 2014-0588-0021-0000
- Page Start:
- 3802
- Page End:
- 3807
- Publication Date:
- 2014-09-12
- Subjects:
- TM -- transmembrane -- DPC -- dodecylphosphocholine -- TMD -- isolated transmembrane domain -- TLR -- toll-like receptor -- TFE -- trifluoroethanol -- TIR -- Toll-interleukin I receptor domain -- NOE -- nuclear overhauser effect -- NOESY -- NOE spectroscopy -- ECD -- extracellular domain -- PAMP -- patogen-associated molecular patterns -- FOS-16 -- hexadecylphosphocholine -- LPR -- lipid-to-protein ratio -- Toll-like receptor -- Transmembrane domain -- Spatial structure -- Dimerization -- Free energy
Biochemistry -- Periodicals
Biophysics -- Periodicals
Molecular biology -- Periodicals
Biochimie -- Périodiques
Biochemistry
Biophysics
Molecular biology
Periodicals
572.05 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00145793 ↗
http://febs.onlinelibrary.wiley.com/hub/journal/10.1002/(ISSN)1873-3468/ ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.febslet.2014.08.031 ↗
- Languages:
- English
- ISSNs:
- 0014-5793
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3901.600000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 1604.xml