2MK9
Spatial structure of the dimeric transmembrane domain of Toll-like receptor 3
Summary for 2MK9
| Entry DOI | 10.2210/pdb2mk9/pdb |
| Related | 2MKA |
| NMR Information | BMRB: 19764 |
| Descriptor | Toll-like receptor 3 (1 entity in total) |
| Functional Keywords | transmembrane domain, dimer, immune system |
| Biological source | Homo sapiens (human) |
| Cellular location | Endoplasmic reticulum membrane; Single-pass type I membrane protein: O15455 |
| Total number of polymer chains | 2 |
| Total formula weight | 8179.89 |
| Authors | Mineev, K.S.,Goncharuk, S.A.,Arseniev, A.S. (deposition date: 2014-02-04, release date: 2014-09-17, Last modification date: 2024-05-15) |
| Primary citation | Mineev, K.S.,Goncharuk, S.A.,Arseniev, A.S. Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: An NMR structural study. Febs Lett., 588:3802-3807, 2014 Cited by PubMed 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. PubMed: 25217833DOI: 10.1016/j.febslet.2014.08.031 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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