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CORDIS

Structural basis of nicotinic acetylcholine receptor function (NICOTINIC RECEPTORS)

Ziel

We aim to determine the 3D structure of the prototypic neurotransmitter receptor, the nicotinic acetylcholinereceptor (Ache), at high resolution, for understanding the structural basis of its function, using advanced electron and X-ray crystallography, NMR, AFM, molecular modelling and electro physiology, combined with antibody and legend labelling. The best available image of a neurotransmitter receptor is that of the Ache at 4.6AA resolution, obtained by partner 2. Our objectives are to achieve:
a. high resolution structure of closed and open Ache channels by electron microscopy;
b. imaging individual Aches in action by AFM;
c. X-ray structure of Ache channels;
d. conformation (by NMR and X-ray crystallography) of Ache fragments;
e. characterization of legend and protein binding properties;
f. detailed models of Torpedo and human Aches byte combined results, rational design of subtype-specific legends and legend assessment by electro physiology. Elucidation of the structure-function relationship of Aches will be catalytic to numerous studies in synapse function and dysfunction.

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HELLENIC PASTEUR INSTITUTE
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127,Vassilissis Sofias Av. 127
11521 ATHENS
Griechenland

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Beteiligte (6)