Bungarotoxin
From Proteopedia
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- | <StructureSection load='1hc9' size='450' side='right' scene='42/423360/Cv/ | + | <StructureSection load='1hc9' size='450' side='right' scene='42/423360/Cv/5' caption='α-Bungarotoxin (green) complex with peptide derived from acetylcholine receptor (yellow) and I- ion (PDB code [[1hc9]])'> |
[[Bungarotoxin|Bungarotoxins]]. α-Bungarotoxin (α-BGT), β-Bungarotoxin (β-BGT), γ-Bungarotoxin (γ-BGT) and κ-Bungarotoxin (κ-BGT) are snake toxins from banded krait.<br /> | [[Bungarotoxin|Bungarotoxins]]. α-Bungarotoxin (α-BGT), β-Bungarotoxin (β-BGT), γ-Bungarotoxin (γ-BGT) and κ-Bungarotoxin (κ-BGT) are snake toxins from banded krait.<br /> | ||
* '''α-BGT''' binds irreversibly to the acetylcholine receptor (AChR) causing paralysis and death. See details in [[Alpha-bungarotoxin]].<br /> | * '''α-BGT''' binds irreversibly to the acetylcholine receptor (AChR) causing paralysis and death. See details in [[Alpha-bungarotoxin]].<br /> | ||
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For toxins in Proteopedia see [[Toxins]]. | For toxins in Proteopedia see [[Toxins]]. | ||
- | <scene name='42/423360/Cv/ | + | <scene name='42/423360/Cv/4'>Iod coordination site</scene> in α-Bungarotoxin (PDB code [[1hc9]]).<ref>PMID:11683996</ref> Water molecule shown as red sphere. |
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== 3D Structures of Bungarotoxin == | == 3D Structures of Bungarotoxin == | ||
- | + | [[Bungarotoxin 3D structures]] | |
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- | + | </StructureSection> | |
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- | **[[2qc1]] – α-BGT+mAChR α subunit <br /> | ||
- | **[[4hqp]] - α−BGT+ AChR α7 subunit<br /> | ||
- | **[[4uy2]] - α−BGT+ AChR α9 subunit<br /> | ||
- | }} | ||
== References == | == References == | ||
+ | <references/> | ||
[[Alpha-bungarotoxin]] | [[Alpha-bungarotoxin]] | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
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References
- ↑ Harel M, Kasher R, Nicolas A, Guss JM, Balass M, Fridkin M, Smit AB, Brejc K, Sixma TK, Katchalski-Katzir E, Sussman JL, Fuchs S. The binding site of acetylcholine receptor as visualized in the X-Ray structure of a complex between alpha-bungarotoxin and a mimotope peptide. Neuron. 2001 Oct 25;32(2):265-75. PMID:11683996