5jmc

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==Receptor binding domain of Botulinum neurotoxin A in complex with rat SV2C==
==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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<StructureSection load='5jmc' size='340' side='right'caption='[[5jmc]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
== Structural highlights ==
== 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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<table><tr><td colspan='2'>[[5jmc]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5JMC FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.64&#8491;</td></tr>
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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'>[https://proteopedia.org/fgij/fg.htm?mol=5jmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jmc OCA], [https://pdbe.org/5jmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jmc RCSB], [https://www.ebi.ac.uk/pdbsum/5jmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jmc ProSAT]</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jmc ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== 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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[https://www.uniprot.org/uniprot/BXA1_CLOBH BXA1_CLOBH] 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5jmc" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5jmc" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bontoxilysin]]
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[[Category: Clostridium botulinum]]
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[[Category: Bagramyan, K]]
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[[Category: Large Structures]]
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[[Category: Dong, M]]
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[[Category: Rattus norvegicus]]
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[[Category: Jin, R]]
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[[Category: Bagramyan K]]
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[[Category: Kalkum, M]]
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[[Category: Dong M]]
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[[Category: Lam, K]]
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[[Category: Jin R]]
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[[Category: Mahrhold, S]]
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[[Category: Kalkum M]]
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[[Category: Perry, K]]
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[[Category: Lam K]]
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[[Category: Rummel, A]]
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[[Category: Mahrhold S]]
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[[Category: Stern, D]]
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[[Category: Perry K]]
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[[Category: Yao, G]]
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[[Category: Rummel A]]
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[[Category: Zhang, S]]
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[[Category: Stern D]]
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[[Category: Hydrolase]]
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[[Category: Yao G]]
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[[Category: Zhang S]]

Current revision

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

PDB ID 5jmc

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