Need info: ACH receptor conformation!

C Wood bsscw at
Tue Dec 5 19:08:21 EST 1995

allosteric effects ... the French scientist that noticed this effect got 
the Noble prize ... he also happens to be very keen on publishing papers 
on the nAChR (nicotinic acetylcholine receptor).  Cheveureux (spelling is 
off .... I will look up a key review paper of his group).  

Dr. Chris Wood PhD
Email: bsscw at
Biochem Dept., Bath Uni.,
Bath, BA2 7AY, UK
Tel work: UK 01225-826826 
          ext 5118 

On 4 Dec 1995, Keith Bradnam wrote:

> Jeremy Hamlet Bremen wrote...
> >...How does the binding of one acetylcholine molecule to its post-synaptic 
> > membrane receptor change the conformation of that receptor to improve the 
> > binding affinity of a second acetylcholine molecule to the same receptor
> > protein? 
> >...
> In a related family of receptors, the ionotropic glutamate receptors (iGluRs),
> the binding of the neurotransmitter (glutamtate) occurs in a quite distinct
> binding domain.  This domain seems to be bilobate in structure.   The ligand
> binds to the larger lobe and this induces conformational changes so that the
> second lobe closes around the ligand.  This has been termed the "venus fly
> trap" model. After the ligand has been sequestered away, there are presumably
> new residues that are available to make binding interactions.  The iGluRs are
> also pentameric and also bind another ligand.  As I recall, one ligand has to
> bind first which then makes a conformational change so that the second ligand
> can bind.  Both of the binding domains have this bilobate structure.
> Maybe something similar happens with the AChR.
> O'Hara et al., Neuron, 11, pp. 41-52 is a good general reference on the nature
> of these binding domains.
> Hope this helps,
> Keith

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