+検索条件
-Structure paper
タイトル | The structure of the tetanus toxin reveals pH-mediated domain dynamics. |
---|---|
ジャーナル・号・ページ | EMBO Rep, Vol. 18, Issue 8, Page 1306-1317, Year 2017 |
掲載日 | 2017年6月23日 |
![]() | Geoffrey Masuyer / Julian Conrad / Pål Stenmark / ![]() |
PubMed 要旨 | The tetanus neurotoxin (TeNT) is a highly potent toxin produced by that inhibits neurotransmission of inhibitory interneurons, causing spastic paralysis in the tetanus disease. TeNT differs from the ...The tetanus neurotoxin (TeNT) is a highly potent toxin produced by that inhibits neurotransmission of inhibitory interneurons, causing spastic paralysis in the tetanus disease. TeNT differs from the other clostridial neurotoxins by its unique ability to target the central nervous system by retrograde axonal transport. The crystal structure of the tetanus toxin reveals a "closed" domain arrangement stabilised by two disulphide bridges, and the molecular details of the toxin's interaction with its polysaccharide receptor. An integrative analysis combining X-ray crystallography, solution scattering and single particle electron cryo-microscopy reveals pH-mediated domain rearrangements that may give TeNT the ability to adapt to the multiple environments encountered during intoxication, and facilitate binding to distinct receptors. |
![]() | ![]() ![]() ![]() |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.6 - 4.5 Å |
構造データ | ![]() EMDB-3588: ![]() PDB-5n0b: ![]() PDB-5n0c: |
化合物 | ![]() ChemComp-ZN: ![]() ChemComp-PEG: ![]() ChemComp-HOH: |
由来 |
|
![]() | TOXIN / Tetanus neurotoxin / tetanospasmin / tentoxilysin / clostridial toxin |