2qc1
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2qc1 |SIZE=350|CAPTION= <scene name='initialview01'>2qc1</scene>, resolution 1.94Å | |PDB= 2qc1 |SIZE=350|CAPTION= <scene name='initialview01'>2qc1</scene>, resolution 1.94Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=LYS:LYSINE'>LYS</scene> | + | |LIGAND= <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Chrna1, Acra ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Chrna1, Acra ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qc1 OCA], [http://www.ebi.ac.uk/pdbsum/2qc1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qc1 RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Wang, Z.]] | [[Category: Wang, Z.]] | ||
[[Category: Yao, Y.]] | [[Category: Yao, Y.]] | ||
| - | [[Category: LYS]] | ||
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
[[Category: buried hydrophilic residue]] | [[Category: buried hydrophilic residue]] | ||
| Line 36: | Line 38: | ||
[[Category: protein binding]] | [[Category: protein binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:47:32 2008'' |
Revision as of 01:47, 31 March 2008
| |||||||
| , resolution 1.94Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | Chrna1, Acra (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the extracellular domain of the nicotinic acetylcholine receptor 1 subunit bound to alpha-bungarotoxin at 1.9 A resolution
Overview
We determined the crystal structure of the extracellular domain of the mouse nicotinic acetylcholine receptor (nAChR) alpha1 subunit bound to alpha-bungarotoxin at 1.94 A resolution. This structure is the first atomic-resolution view of a nAChR subunit extracellular domain, revealing receptor-specific features such as the main immunogenic region (MIR), the signature Cys-loop and the N-linked carbohydrate chain. The toxin binds to the receptor through extensive protein-protein and protein-sugar interactions. To our surprise, the structure showed a well-ordered water molecule and two hydrophilic residues deep in the core of the alpha1 subunit. The two hydrophilic core residues are highly conserved in nAChRs, but correspond to hydrophobic residues in the nonchannel homolog acetylcholine-binding proteins. We carried out site-directed mutagenesis and electrophysiology analyses to assess the functional role of the glycosylation and the hydrophilic core residues. Our structural and functional studies show essential features of the nAChR and provide new insights into the gating mechanism.
About this Structure
2QC1 is a Protein complex structure of sequences from Bungarus multicinctus and Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution., Dellisanti CD, Yao Y, Stroud JC, Wang ZZ, Chen L, Nat Neurosci. 2007 Aug;10(8):953-62. Epub 2007 Jul 22. PMID:17643119
Page seeded by OCA on Mon Mar 31 04:47:32 2008
