5jlv: Difference between revisions
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==Receptor binding domain of Botulinum neurotoxin A in complex with human glycosylated SV2C== | |||
<StructureSection load='5jlv' size='340' side='right' caption='[[5jlv]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5jlv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JLV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JLV FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
[[Category: | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jlv OCA], [http://pdbe.org/5jlv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jlv RCSB], [http://www.ebi.ac.uk/pdbsum/5jlv PDBsum]</span></td></tr> | |||
</table> | |||
== 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). | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bontoxilysin]] | |||
[[Category: Bagramyan, K]] | |||
[[Category: Dong, M]] | [[Category: Dong, M]] | ||
[[Category: | [[Category: Jin, R]] | ||
[[Category: | [[Category: Kalkum, M]] | ||
[[Category: Lam, K]] | |||
[[Category: Mahrhold, S]] | [[Category: Mahrhold, S]] | ||
[[Category: Perry, K]] | [[Category: Perry, K]] | ||
[[Category: Rummel, A]] | [[Category: Rummel, A]] | ||
[[Category: | [[Category: Stern, D]] | ||
[[Category: Yao, G]] | |||
[[Category: Zhang, S]] | |||
[[Category: Botulinum neurotoxin]] | |||
[[Category: Glycosylation]] | |||
[[Category: Hydrolase]] | |||
[[Category: Receptor binding domain]] | |||
