Human 5-HT3A -- Thr 82

Species Original Mutated to Mutation
Human Thr 82  

 

Rat Equivalent Thr 81    
Mouse Equivalent Thr 87 Ala T87A

 

mThr87Ala

Nine residues (Thr 86, Thr 87, Tyr 88, Ile 89, Tyr 91, Arg 92, Gln 93, Tyr 94, Trp 95) were mutated individually to alanine (alanine scanning mutagenesis. [3H]granisetron, curare, and serotonin were used as the ligands to examine binding.

W90F was analyzed instead of W90A, and it proved to be the only mutation that significantly affected the interaction of curare with the receptor. R92A was the only substitution that altered the affinity of serotonin. W90F, R92A, and Y94A all reduced the affinity of [3H]granisetron. The periodicity of this effect suggests the involvement of a beta-strand.

 

Yan D, Schulte MK, Bloom KE, White MM (1999) Structural Features of the Ligand-binding Domain of the Serotonin 5HT3 Receptor. The Journal of Biological Chemistry 274 (9): 5537-5541

 

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