5jmc

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'''Unreleased structure'''
 
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The entry 5jmc is ON HOLD until Paper Publication
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==Receptor binding domain of Botulinum neurotoxin A in complex with rat SV2C==
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<StructureSection load='5jmc' size='340' side='right' caption='[[5jmc]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
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Authors: Yao, G., Zhang, S., Mahrhold, S., Lam, K., Stern, D., Bagramyan, K., Perry, K., Kalkum, M., Rummel, A., Dong, M., Jin, R.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5jmc]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JMC FirstGlance]. <br>
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Description: Receptor binding domain of Botulinum neurotoxin A in complex with rat SV2C
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jlv|5jlv]]</td></tr>
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[[Category: Unreleased Structures]]
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<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>
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<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=5jmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jmc OCA], [http://pdbe.org/5jmc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jmc RCSB], [http://www.ebi.ac.uk/pdbsum/5jmc PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[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_RAT SV2C_RAT]] 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. Receptor for the botulinium neurotoxin type A/BOTA.
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__TOC__
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</StructureSection>
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[[Category: Bontoxilysin]]
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[[Category: Bagramyan, K]]
[[Category: Dong, M]]
[[Category: Dong, M]]
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[[Category: Yao, G]]
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[[Category: Jin, R]]
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[[Category: Zhang, S]]
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[[Category: Kalkum, M]]
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[[Category: Lam, K]]
[[Category: Mahrhold, S]]
[[Category: Mahrhold, S]]
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[[Category: Bagramyan, K]]
 
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[[Category: Lam, K]]
 
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[[Category: Kalkum, M]]
 
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[[Category: Stern, D]]
 
[[Category: Perry, K]]
[[Category: Perry, K]]
[[Category: Rummel, A]]
[[Category: Rummel, A]]
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[[Category: Jin, R]]
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[[Category: Stern, D]]
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[[Category: Yao, G]]
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[[Category: Zhang, S]]
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[[Category: Hydrolase]]

Revision as of 22:28, 20 June 2016

Receptor binding domain of Botulinum neurotoxin A in complex with rat SV2C

5jmc, resolution 2.64Å

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