Binding site of AChR
From Proteopedia
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<StructureSection load='1hc9' size='450' side='right' background='none' caption='structure of binding site of AChR' scene='' > | <StructureSection load='1hc9' size='450' side='right' background='none' caption='structure of binding site of AChR' scene='' > | ||
There are two kinds of acetylcholine receptor in nature: [http://en.wikipedia.org/wiki/Nicotinic_acetylcholine_receptor nicotinic acetylcholine receptors] and [http://en.wikipedia.org/wiki/Muscarinic_acetylcholine_receptor muscarinic acetylcholine receptors]. We should notice that the mAChRs are not ion channels, but belong instead to the superfamily of G-protein-coupled receptors that activate other ionic channels via a second messenger cascade. So in this page we just talk about the nAChR. | There are two kinds of acetylcholine receptor in nature: [http://en.wikipedia.org/wiki/Nicotinic_acetylcholine_receptor nicotinic acetylcholine receptors] and [http://en.wikipedia.org/wiki/Muscarinic_acetylcholine_receptor muscarinic acetylcholine receptors]. We should notice that the mAChRs are not ion channels, but belong instead to the superfamily of G-protein-coupled receptors that activate other ionic channels via a second messenger cascade. So in this page we just talk about the nAChR. | ||
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== Pentameric ligand-gated ion channel == | == Pentameric ligand-gated ion channel == | ||
| - | Pentameric ligand gated ion channels(<scene name='68/688431/Plgics/1'>pLGICs</scene>), or Cys-loop receptors,mediate rapid chemical transmission of signals. Nicotinic acetylcholine receptor is a kind of pentameric ligand gated ion channels. So at first of this page, we introduce some facts of the pentameric ligand gated ion channels, which will help us to understand the structure and function of AChR. | + | Pentameric ligand gated ion channels(<scene name='68/688431/Plgics/1'>pLGICs</scene>), or [http://en.wikipedia.org/wiki/Cys-loop_receptors Cys-loop receptors],mediate rapid chemical transmission of signals. Nicotinic acetylcholine receptor is a kind of pentameric ligand gated ion channels. So at first of this page, we introduce some facts of the pentameric ligand gated ion channels, which will help us to understand the structure and function of AChR. |
== Acetylcholine receptor == | == Acetylcholine receptor == | ||
| + | The nAChR is unable to bind ACh when bound to any of the snake venom α-neurotoxins. These α-neurotoxins antagonistically bind tightly and noncovalently to nAChRs of skeletal muscles, thereby blocking the action of ACh at the postsynaptic membrane, inhibiting ion flow and leading to paralysis and death. The nAChR contains two binding sites for snake venom neurotoxins. Progress towards discovering the dynamics of binding action of these sites has proved difficult, although recent studies using normal mode dynamics[13] have aided in predicting the nature of both the binding mechanisms of snake toxins and of ACh to nAChRs. These studies have shown that a twist-like motion caused by ACh binding is likely responsible for pore opening, and that one or two molecules of α-bungarotoxin (or other long-chain α-neurotoxin) suffice to halt this motion. The toxins seem to lock together neighboring receptor subunits, inhibiting the twist and therefore, the opening motion.<ref>PMID:18327915</ref> | ||
== Acetylcholine binding protein == | == Acetylcholine binding protein == | ||
Revision as of 14:16, 18 January 2015
Structure and Function about Binding Site of Acetylcholine Receptor
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Samson AO, Levitt M. Inhibition mechanism of the acetylcholine receptor by alpha-neurotoxins as revealed by normal-mode dynamics. Biochemistry. 2008 Apr 1;47(13):4065-70. doi: 10.1021/bi702272j. Epub 2008 Mar 8. PMID:18327915 doi:http://dx.doi.org/10.1021/bi702272j
Proteopedia Page Contributors and Editors (what is this?)
Ma Zhuang, Zicheng Ye, Angel Herraez, Alexander Berchansky, Michal Harel
