GPCR dimerisation

Recently, dimerisation has been reported in a number of Class Class 

Phe— Ala mutation. The G276A, G280A, L284A and Y209A mutations all resulted in a positive free energy change. These results are consistent with the idea that these mutations destabilise the dimer interface, resulting in mutations that inhibit G-protein activation due to the inability of the receptor to form dimers.  

There are clear relationships between CMA and the ET analysis. However, the ET method appears to give clearer results. Consequently, the ET method was used to 

Molecular basis of receptor/G-protein-coupling selectivity. Pharmacol. Ther., 1998, 80, 231-264. 

Watson, S., Arkinstall, S. The G-protein linked receptor facts book, Academic Press, London, 1994. 

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On the basis of these results eombined with experimental data, a model of the receptor-G-protein complex was constructed. The reeeptor was orientated so that il3 and il4. fomied by palmitoylation of two eysteines in the C-terminal, were in eontact distance of Gpy. This left the first eluster as the primary interaetion site for ill and ill. The analysis of these results in the light of reeent work on GPCR dimerisation has led to some interesting results (see below). 

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