1bun
From Proteopedia
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| - | [[Image:1bun.gif|left|200px]] | + | [[Image:1bun.gif|left|200px]] |
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| - | '''STRUCTURE OF BETA2-BUNGAROTOXIN: POTASSIUM CHANNEL BINDING BY KUNITZ MODULES AND TARGETED PHOSPHOLIPASE ACTION''' | + | {{Structure |
| + | |PDB= 1bun |SIZE=350|CAPTION= <scene name='initialview01'>1bun</scene>, resolution 2.45Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF BETA2-BUNGAROTOXIN: POTASSIUM CHANNEL BINDING BY KUNITZ MODULES AND TARGETED PHOSPHOLIPASE ACTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BUN is a [ | + | 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]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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] |
[[Category: Bungarus multicinctus]] | [[Category: Bungarus multicinctus]] | ||
[[Category: Phospholipase A(2)]] | [[Category: Phospholipase A(2)]] | ||
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[[Category: presynaptic neurotoxin]] | [[Category: presynaptic neurotoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:15:58 2008'' |
Revision as of 08:15, 20 March 2008
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| , resolution 2.45Å | |||||||
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| Ligands: | |||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF BETA2-BUNGAROTOXIN: POTASSIUM CHANNEL BINDING BY KUNITZ MODULES AND TARGETED PHOSPHOLIPASE ACTION
Overview
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.
About this Structure
1BUN is a Protein complex structure of sequences from Bungarus multicinctus. Full crystallographic information is available from OCA.
Reference
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
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