1bun

From Proteopedia

(Difference between revisions)

Revision as of 02:52, 11 September 2015

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

Structural highlights

1bun is a 2 chain structure with sequence from Bungarus multicinctus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Phospholipase A(2), with EC number 3.1.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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. [VKTH2_BUNMU] Beta-2-bungarotoxin is a presynaptic neurotoxin of the venom. The B chain is homologous to venom basic protease inhibitors but has no protease inhibitor activity and blocks voltage-gated potassium channels (Kv).^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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:8590005^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wu PF, Wu SN, Chang CC, Chang LS. Cloning and functional expression of B chains of beta-bungarotoxins from Bungarus multicinctus (Taiwan banded krait). Biochem J. 1998 Aug 15;334 ( Pt 1):87-92. PMID:9693106
↑ Kwong PD, McDonald NQ, Sigler PB, Hendrickson WA. Structure of beta 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action. Structure. 1995 Oct 15;3(10):1109-19. PMID:8590005

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bun"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=1bun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bun RCSB], [http://www.ebi.ac.uk/pdbsum/1bun PDBsum]</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=1bun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bun OCA], [http://pdbe.org/1bun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bun RCSB], [http://www.ebi.ac.uk/pdbsum/1bun PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PA21B_BUNMU PA21B_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. [[http://www.uniprot.org/uniprot/IVB2_BUNMU IVB2_BUNMU]] Beta-2-bungarotoxin is a presynaptic neurotoxin of the venom. The B chain is homologous to venom basic protease inhibitors but has no protease inhibitor activity and blocks voltage-gated potassium channels (Kv).<ref>PMID:9693106</ref>
+[[http://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. [[http://www.uniprot.org/uniprot/VKTH2_BUNMU VKTH2_BUNMU]] Beta-2-bungarotoxin is a presynaptic neurotoxin of the venom. The B chain is homologous to venom basic protease inhibitors but has no protease inhibitor activity and blocks voltage-gated potassium channels (Kv).<ref>PMID:9693106</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1bun" style="background-color:#fffaf0;"></div>
 ==See Also==

1bun

From Proteopedia

Revision as of 02:52, 11 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox