1l4w
From Proteopedia
(New page: 200px<br /><applet load="1l4w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l4w" /> '''NMR structure of an AChR-peptide (Torpedo Ca...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1l4w.gif|left|200px]]<br /><applet load="1l4w" size=" | + | [[Image:1l4w.gif|left|200px]]<br /><applet load="1l4w" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l4w" /> | caption="1l4w" /> | ||
'''NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin'''<br /> | '''NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of a peptide corresponding to residues 182-202 of the | + | The structure of a peptide corresponding to residues 182-202 of the acetylcholine receptor alpha1 subunit in complex with alpha-bungarotoxin was solved using NMR spectroscopy. The peptide contains the complete sequence of the major determinant of AChR involved in alpha-bungarotoxin binding. One face of the long beta hairpin formed by the AChR peptide consists of exposed nonconserved residues, which interact extensively with the toxin. Mutations of these receptor residues confer resistance to the toxin. Conserved AChR residues form the opposite face of the beta hairpin, which creates the inner and partially hidden pocket for acetylcholine. An NMR-derived model for the receptor complex with two alpha-bungarotoxin molecules shows that this pocket is occupied by the conserved alpha-neurotoxin residue R36, which forms cation-pi interactions with both alphaW149 and gammaW55/deltaW57 of the receptor and mimics acetylcholine. |
==About this Structure== | ==About this Structure== | ||
| - | 1L4W is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http:// | + | 1L4W is a [http://en.wikipedia.org/wiki/Protein_complex 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=1L4W OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 16: | ||
[[Category: Eisenstein, M.]] | [[Category: Eisenstein, M.]] | ||
[[Category: Rodriguez, E.]] | [[Category: Rodriguez, E.]] | ||
| - | [[Category: Samson, A | + | [[Category: Samson, A O.]] |
[[Category: Scherf, T.]] | [[Category: Scherf, T.]] | ||
[[Category: acetylcholine receptor]] | [[Category: acetylcholine receptor]] | ||
| Line 23: | Line 23: | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:23 2008'' |
Revision as of 11:41, 21 February 2008
|
NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin
Overview
The structure of a peptide corresponding to residues 182-202 of the acetylcholine receptor alpha1 subunit in complex with alpha-bungarotoxin was solved using NMR spectroscopy. The peptide contains the complete sequence of the major determinant of AChR involved in alpha-bungarotoxin binding. One face of the long beta hairpin formed by the AChR peptide consists of exposed nonconserved residues, which interact extensively with the toxin. Mutations of these receptor residues confer resistance to the toxin. Conserved AChR residues form the opposite face of the beta hairpin, which creates the inner and partially hidden pocket for acetylcholine. An NMR-derived model for the receptor complex with two alpha-bungarotoxin molecules shows that this pocket is occupied by the conserved alpha-neurotoxin residue R36, which forms cation-pi interactions with both alphaW149 and gammaW55/deltaW57 of the receptor and mimics acetylcholine.
About this Structure
1L4W is a Protein complex structure of sequences from Bungarus multicinctus. Full crystallographic information is available from OCA.
Reference
The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR., Samson A, Scherf T, Eisenstein M, Chill J, Anglister J, Neuron. 2002 Jul 18;35(2):319-32. PMID:12160749
Page seeded by OCA on Thu Feb 21 13:41:23 2008
