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J. Biol. Chem., Vol. 268, Issue 2, 909-916, Jan, 1993
L Pillet, O Tremeau, F Ducancel, P Drevet, S Zinn-Justin, S Pinkasfeld, JC Boulain and A Menez
To study the site by which erabutoxin a (Ea) from Laticauda semifasciata
binds to the nicotinic acetylcholine receptor, we mutated most residues
that are shared with other curaremimetic toxins and studied the structural
and biological consequences of introduced mutations. By site-directed
mutagenesis, we changed Ser-8 into Gly (EaS8G), Lys-27 into Glu (EaK27E),
Trp-29 into Phe (EaW29F) and His (EaW29H), Asp-31 into His (EaD31H), Phe-32
into Leu (EaF32L), Arg-33 into Lys (EaR33K) and Glu (EaR33E), Gly-34 into
Ser (EaG34S), Glu-38 into Gln (EaE38Q) and Lys (EaE38K), Gly-49 into Val
(EaG49V), and Leu- 52 into Ala (EaL52A). All mutants were homogeneous as
judged by various analytical procedures. EaE38Q, EaG49V, and EaL52A bound
the nicotinic acetylcholine receptor with apparent Kd values close to
10(-10) M, virtually identical to wild Ea. Therefore, Glu-38, Gly-49, and
Leu-52 are not important elements in the expression of curaremimetic
function in Ea. Mutations of Phe-32 and Gly-34 provoked a 7-fold affinity
decrease, suggesting that these residues moderately contribute to function.
The 176-fold affinity decrease due to mutation of Ser-8 may reflect some
structural change that operates in the polypeptide chain of the mutant, as
detected by circular dichroism. Decreases in affinity by a factor of 175,
67, 46, and 318 were seen upon mutations of Lys-27 into Glu, Trp-29 into
Phe, Asp-31 into His, and Arg-33 into Glu, with no concomitant change in
secondary structure. These residues appear to be important elements of the
curaremimetic function of Ea. Thus, a picture of the contribution of
conserved residues to the function of a curaremimetic toxin is proposed on
the basis of experimental evidence.
Genetic engineering of snake toxins. Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis
Departement d'Ingenierie et d'Etudes des Proteines, Centre d'Etudes de Saclay, Commissariat a l'Energie Atomique, Gif-sur-Yvette, France.
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