Binding site of AChR: Difference between revisions

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Ma Zhuang, Zicheng Ye, Michal Harel, Angel Herraez, Alexander Berchansky

Revision as of 14:56, 2 February 2015 view source Ma Zhuang (talk \| contribs) 217 edits No edit summary ← Older edit		Revision as of 14:59, 2 February 2015 view source Ma Zhuang (talk \| contribs) 217 edits No edit summary Newer edit →
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	[[Image:M2 helices.PNG\|thumb\|210px\|Fig. 2. Top view of GLIC M2 helices\|left]]		[[Image:M2 helices.PNG\|thumb\|210px\|Fig. 2. Top view of GLIC M2 helices\|left]]

	X-ray structure of homologues of the extracellular domain(ECD) of nAChRs have also been described:the acetylcholine binding protein(AChBP) co-crystallized with agonists and antagonists, and the ECD of α1-nAChRs. Most pLGICs undergo desensitization on prolonged exposure to agonist, complicating structural investigations of the transient open conformation. <ref>PMID:18987633</ref> The overall architecture of bacterial Gloeobacter violaceus pentameric ligand-gated ion(GLIC) is similar to nAChR(Fig 1). The five subunits are arranged in a barrel-like manner around a central symmetry axis that coincides with the ion permeation pathway.<ref>PMID:18987633</ref> The transmembrane domain of each subunit consists of four helices and M2 helices form the wall of the pore.		X-ray structure of homologues of the extracellular domain(ECD) of nAChRs have also been described:the acetylcholine binding protein(AChBP) co-crystallized with agonists and antagonists, and the ECD of α1-nAChRs. Most pLGICs undergo desensitization on prolonged exposure to agonist, complicating structural investigations of the transient open conformation. <ref>PMID:18987633</ref> The overall architecture of bacterial Gloeobacter violaceus pentameric ligand-gated ion(GLIC) is similar to nAChR(Fig 1). The five subunits are arranged in a barrel-like manner around a central symmetry axis that coincides with the ion permeation pathway.<ref>PMID:18987633</ref> The transmembrane domain of each subunit consists of four helices and M2 helices form the wall of the pore(Fig 2).Figure 2 shows that helix backbones and side chains facing the pore are depicted. Hydrophobic, polar and negative residues are coloured yellow, green and red respectively.