4jra
From Proteopedia
Line 1: | Line 1: | ||
- | + | {{STRUCTURE_4jra| PDB=4jra | SCENE= }} | |
+ | ===CRYSTAL STRUCTURE OF THE BOTULINUM NEUROTOXIN A RECEPTOR-BINDING DOMAIN IN COMPLEX WITH THE LUMINAL DOMAIN Of SV2C=== | ||
- | The | + | ==Function== |
+ | [[http://www.uniprot.org/uniprot/BXA1_CLOBO BXA1_CLOBO]] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure. [[http://www.uniprot.org/uniprot/SV2C_HUMAN SV2C_HUMAN]] Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity). | ||
- | + | ==About this Structure== | |
- | + | [[4jra]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JRA OCA]. | |
- | + | [[Category: Bontoxilysin]] | |
+ | [[Category: Benoit, R M.]] | ||
+ | [[Category: Capitani, G.]] | ||
+ | [[Category: Frey, D.]] | ||
+ | [[Category: Jaussi, R.]] | ||
+ | [[Category: Kammerer, R A.]] | ||
+ | [[Category: Schertler, G F.X.]] | ||
+ | [[Category: Wieser, M M.]] | ||
+ | [[Category: Beta-helix]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Lumen]] | ||
+ | [[Category: Toxin]] | ||
+ | [[Category: Vesicle]] |
Revision as of 13:43, 20 November 2013
CRYSTAL STRUCTURE OF THE BOTULINUM NEUROTOXIN A RECEPTOR-BINDING DOMAIN IN COMPLEX WITH THE LUMINAL DOMAIN Of SV2C
Function
[BXA1_CLOBO] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure. [SV2C_HUMAN] Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity).
About this Structure
4jra is a 4 chain structure. Full crystallographic information is available from OCA.
Categories: Bontoxilysin | Benoit, R M. | Capitani, G. | Frey, D. | Jaussi, R. | Kammerer, R A. | Schertler, G F.X. | Wieser, M M. | Beta-helix | Hydrolase | Lumen | Toxin | Vesicle