8AR1
Solution structure of TLR3 transmembrane and cytoplasmic juxtamembrane regions
Summary for 8AR1
| Entry DOI | 10.2210/pdb8ar1/pdb |
| NMR Information | BMRB: 34751 |
| Descriptor | Toll-like receptor 3 (1 entity in total) |
| Functional Keywords | protein, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 6043.17 |
| Authors | Kornilov, F.D.,Shabalkina, A.V.,Goncharuk, M.V.,Goncharuk, S.A.,Arseniev, A.S.,Mineev, K.S. (deposition date: 2022-08-15, release date: 2023-03-22, Last modification date: 2024-06-19) |
| Primary citation | Kornilov, F.D.,Shabalkina, A.V.,Lin, C.,Volynsky, P.E.,Kot, E.F.,Kayushin, A.L.,Lushpa, V.A.,Goncharuk, M.V.,Arseniev, A.S.,Goncharuk, S.A.,Wang, X.,Mineev, K.S. The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors. Nat Commun, 14:1503-1503, 2023 Cited by PubMed Abstract: Toll-like receptors (TLRs) are the important participants of the innate immune response. Their spatial organization is well studied for the ligand-binding domains, while a lot of questions remain unanswered for the membrane and cytoplasmic regions of the proteins. Here we use solution NMR spectroscopy and computer simulations to investigate the spatial structures of transmembrane and cytoplasmic juxtamembrane regions of TLR2, TLR3, TLR5, and TLR9. According to our data, all the proteins reveal the presence of a previously unreported structural element, the cytoplasmic hydrophobic juxtamembrane α-helix. As indicated by the functional tests in living cells and bioinformatic analysis, this helix is important for receptor activation and plays a role, more complicated than a linker, connecting the transmembrane and cytoplasmic parts of the proteins. PubMed: 36932058DOI: 10.1038/s41467-023-37042-6 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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