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1bun

From Proteopedia

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[[Image:1bun.gif|left|200px]]
 
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{{Structure
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==STRUCTURE OF BETA2-BUNGAROTOXIN: POTASSIUM CHANNEL BINDING BY KUNITZ MODULES AND TARGETED PHOSPHOLIPASE ACTION==
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|PDB= 1bun |SIZE=350|CAPTION= <scene name='initialview01'>1bun</scene>, resolution 2.45&Aring;
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<StructureSection load='1bun' size='340' side='right'caption='[[1bun]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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<table><tr><td colspan='2'>[[1bun]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BUN FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span>
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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]] 2.45&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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|DOMAIN=
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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=1bun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bun OCA], [https://pdbe.org/1bun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bun RCSB], [https://www.ebi.ac.uk/pdbsum/1bun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bun ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bun OCA], [http://www.ebi.ac.uk/pdbsum/1bun PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bun RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PA2B1_BUNMU PA2B1_BUNMU] Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1bun_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bun ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF BETA2-BUNGAROTOXIN: POTASSIUM CHANNEL BINDING BY KUNITZ MODULES AND TARGETED PHOSPHOLIPASE ACTION'''
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==See Also==
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*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: beta-bungarotoxin is a heterodimeric neurotoxin consisting of a phospholipase subunit linked by a disulfide bond to a K+ channel binding subunit which is a member of the Kunitz protease inhibitor superfamily. Toxicity, characterized by blockage of neural transmission, is achieved by the lipolytic action of the phospholipase targeted to the presynaptic membrane by the Kunitz module. RESULTS: The crystal structure at 2.45 A resolution suggests that the ion channel binding region of the Kunitz subunit is at the opposite end of the module from the loop typically involved in protease binding. Analysis of the phospholipase subunit reveals a partially occluded substrate-binding surface and reduced hydrophobicity. CONCLUSIONS: Molecular recognition by this Kunitz module appears to diverge considerably from more conventional superfamily members. The ion channel binding region identified here may mimic the regulatory interaction of endogenous neuropeptides. Adaptations of the phospholipase subunit make it uniquely suited to targeting and explain the remarkable ability of the toxin to avoid binding to non-target membranes. Insight into the mechanism of beta-bungarotoxin gained here may lead to the development of therapeutic strategies against not only pathological cells, but also enveloped viruses.
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==About this Structure==
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1BUN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUN OCA].
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==Reference==
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Structure of beta 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action., Kwong PD, McDonald NQ, Sigler PB, Hendrickson WA, Structure. 1995 Oct 15;3(10):1109-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8590005 8590005]
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[[Category: Bungarus multicinctus]]
[[Category: Bungarus multicinctus]]
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[[Category: Phospholipase A(2)]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Hendrickson WA]]
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[[Category: Hendrickson, W A.]]
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[[Category: Kwong PD]]
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[[Category: Kwong, P D.]]
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[[Category: Mcdonald NQ]]
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[[Category: Mcdonald, N Q.]]
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[[Category: Sigler PB]]
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[[Category: Sigler, P B.]]
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[[Category: hydrolase]]
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[[Category: presynaptic neurotoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:08:34 2008''
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Current revision

STRUCTURE OF BETA2-BUNGAROTOXIN: POTASSIUM CHANNEL BINDING BY KUNITZ MODULES AND TARGETED PHOSPHOLIPASE ACTION

PDB ID 1bun

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