Structural highlights
Function
[TETX_CLOTE] Tetanus toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of synaptobrevin-2.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The 2.7 A structure of the tetanus neurotoxin receptor binding fragment Hc reveals a jelly-roll domain and a beta-trefoil domain. Hc retains the unique transport properties of the holotoxin and is capable of eliciting a protective immunological response against the full length holotoxin.
Structure of the receptor binding fragment HC of tetanus neurotoxin.,Umland TC, Wingert LM, Swaminathan S, Furey WF, Schmidt JJ, Sax M Nat Struct Biol. 1997 Oct;4(10):788-92. PMID:9334741[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Umland TC, Wingert LM, Swaminathan S, Furey WF, Schmidt JJ, Sax M. Structure of the receptor binding fragment HC of tetanus neurotoxin. Nat Struct Biol. 1997 Oct;4(10):788-92. PMID:9334741
