Three-Dimensional Solution Structure of α-Conotoxin MII, an α3β2Neuronal Nicotinic Acetylcholine Receptor-Targeted Ligand†,‡

Biochemistry ◽  
1997 ◽  
Vol 36 (50) ◽  
pp. 15693-15700 ◽  
Author(s):  
Ki-Joon Shon ◽  
Steven C. Koerber ◽  
Jean E. Rivier ◽  
Baldomero M. Olivera ◽  
J. Michael McIntosh
Keyword(s):  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Solution Structure ◽  
Three Dimensional ◽  
Dimensional Solution ◽  
Nicotinic Acetylcholine

scholarly journals Three-Dimensional Micro Seconds X-Ray Single Molecule Tracking of Nicotinic Acetylcholine Receptor with Picometer Accuracy

2013 ◽  
Vol 104 (2) ◽  
pp. 543a
Author(s):  
Miki Tokue ◽  
Kentaro Hoshisashi ◽  
Hiroshi Sekiguchi ◽  
Naoto Yagi ◽  
Kohei Ichiyanagi ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Single Molecule ◽  
Three Dimensional ◽  
Nicotinic Acetylcholine ◽  
Single Molecule Tracking ◽  
X Ray

Three-dimensional Image Analysis of Tubular Crystals of Membrane Proteins in Ice

1990 ◽  
Vol 48 (1) ◽  
pp. 242-243
Author(s):  
Chikashi Toyoshima
Keyword(s):  
Image Analysis ◽  
Lipid Bilayer ◽  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Three Dimensional ◽  
Biological Macromolecules ◽  
Nicotinic Acetylcholine ◽  
Dimensional Image ◽  
The Difference ◽  
Tubular Crystals

Frozen-hydrated electron microscopy is a powerful method that allows us to preserve biological macromolecules in physiological ionic conditions and obtain the density (Coulomb potential) maps directly. Changes in quarternary structure in different conditions have been demonstrated using this technique for the gap junction (1) and the nicotinic acetylcholine receptor (2). Since the image contrast originates from the difference in density between the specimen and ice, the method has a considerable advantage over conventional methods in resolving structure inside the lipid bilayer, especially when molecules are arranged in a helical array to form tubular crystals. The molecules in a helical array present many different views to the incident electron beam, hence the electron micrograph actually contains a large amount of three-dimensional information. By using helical image analysis, it is possible to obtain a three-dimensional image from a single micrograph in many instances. Furthermore, the data is complete: There is no "missing cone" problem arising from a limited angle of tilt; the resolution in the reconstructed image is isotropic. The mean (radial) density distribution is available from equatorial data; thus the value in the map is an absolute measure of the density.We have been analysing tubular crystals of the nicotinic acetylcholine receptor from electric ray and the calcium ATPase from rabbit sarcoplasmic reticulum. Helical image analysis at 17 Å resolution of the narrow tubes embedded in ice has allowed two leaflets of the lipid bilayer to be resolved clearly (2). The lipid bilayer was not resolved in previous tilt reconstructions using flattened tubes at a similar (in plane) resolution and up to 60 degrees tilt (3).

scholarly journals Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors

2004 ◽  
Vol 380 (2) ◽  
pp. 347-352 ◽  
Author(s):  
Seung-Wook CHI ◽  
Do-Hyoung KIM ◽  
Baldomero M. OLIVERA ◽  
J. Michael McINTOSH ◽  
Kyou-Hoon HAN
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Solution Structure ◽  
Heavy Atom ◽  
Three Dimensional ◽  
Cone Snail ◽  
Dimensional Solution ◽  
Nicotinic Acetylcholine ◽  
Binding Characteristics ◽  
Molecular Features

α-Conotoxin GIC is a 16-residue peptide isolated from the venom of the cone snail Conus geographus. α-Conotoxin GIC potently blocks the α3β2 subtype of human nicotinic acetylcholine receptor, showing a high selectivity for neuronal versus muscle subtype [McIntosh, Dowell, Watkins, Garrett, Yoshikami, and Olivera (2002) J. Biol. Chem. 277, 33610–33615]. We have now determined the three-dimensional solution structure of α-conotoxin GIC by NMR spectroscopy. The structure of α-conotoxin GIC is well defined with backbone and heavy atom root mean square deviations (residues 2–16) of 0.53 Å and 0.96 Å respectively. Structure and surface comparison of α-conotoxin GIC with the other α4/7 subfamily conotoxins reveals unique structural aspects of α-conotoxin GIC. In particular, the structural comparison between α-conotoxins GIC and MII indicates molecular features that may confer their similar receptor specificity profile, as well as those that provide the unique binding characteristics of α-conotoxin GIC.

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