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TABLE IV

Kinetic Analyses of α127 Homologous Residues in Non–α Subunits

Construct
Agonist
k0 (s−1)
kcobs (s−1)
kccor (s−1)
Keq (ko/kccor)
Normalized Keq (mut/wt)
n
βS127A Cho 53 1296 3460.3 0.015 3.1 
βS127V Cho 108 1305 3484.3 0.030 1.5 
βS127Y Cho 70 850 2269.5 0.030 1.5 
δS129Y ACh 23253 1874 2342.5 9.92 0.35 
εT127A Cho 138 1484 3962.3 0.034 0.74 
εT127V Cho 52 420 1121.4 0.046 1.0 
εT127Y ACh 30370 2550 3187.5 9.52 0.34 
Construct
Agonist
k0 (s−1)
kcobs (s−1)
kccor (s−1)
Keq (ko/kccor)
Normalized Keq (mut/wt)
n
βS127A Cho 53 1296 3460.3 0.015 3.1 
βS127V Cho 108 1305 3484.3 0.030 1.5 
βS127Y Cho 70 850 2269.5 0.030 1.5 
δS129Y ACh 23253 1874 2342.5 9.92 0.35 
εT127A Cho 138 1484 3962.3 0.034 0.74 
εT127V Cho 52 420 1121.4 0.046 1.0 
εT127Y ACh 30370 2550 3187.5 9.52 0.34 

In β, δ, or ε subunit, none of the mutants at residues homologous to Y127 show fold-change in Keq greater than threefold. These residues may not be moving during AChR gating. The abbreviations used here are the same as indicated earlier.

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