Skip to main content
. 2012 Dec;82(6):1136–1149. doi: 10.1124/mol.112.080507

TABLE 2.

SNAP-25 alanine mutants

Residues determined to be important for Gβγ binding to SNAP-25 peptides were successively introduced into the native SNAP-25 sequence. Listed are the names given to each SNAP-25 mutant with the corresponding list of residues mutated to alanine. Residues in boldface are the new mutated residue added to the previously made mutant SNAP-25. Max is the maximum fluorescence enhancement (F1/F0) of the nonlinear regression for the each mutant, normalized to the maximum enhancement for wild-type SNAP-25. The N4A mutant contains only the four alanine mutations near the N terminus of the SNARE complex. Data are means (± S.E.).

Mutant Name Residues of SNAP-25 Mutated Log EC50 EC50 Max
WT N.A. −6.45 (± 0.20) 3.5 × 10−7, (2.2 × 10−7–5.6 × 10−7) 100 (± 15)
2A R198A, K201A −6.18 (± 0.13) 6.6 × 10−7, (4.9 × 10−7–8.9 × 10−7) 96 (± 10)
3A E62A, R198A, K201A −5.93 (± 0.12) 1.2 × 10−6, (8.9 × 10−7–1.5 × 10−6) 122 (± 16)
4A E62A, D99A, R198A, K201A −6.12 (± 0.13) 7.6 × 10−7, (5.6 × 10−7–1.0 × 10−6) 71 (± 8)
5A E62A, D99A, K102A, R198A, K201A −6.08 (± 0.15) 8.3 × 10−7, (5.9 × 10−7–1.7 × 10−6) 70 (± 9)
6A E62A, D99A, K102A, R135A, R198A, K201A −5.97 (± 0.08) 1.1 × 10−6, (7.4 × 10−7–1.2 × 10−6) 88 (± 8)
7A E62A, D99A, K102A, R135A, R136A, R198A, K201A −6.12 (± 0.09) 7.6 × 10−7, (6.2 × 10−7–8.9 × 10−7) 33 (± 3)
8A E62A, D99A, K102A, R135A, R136A, R142A, R198A, K201A −5.87 (± 0.12) 1.3 × 10−6, (1.02 × 10−6–1.8 × 10−6) 20 (± 3)
9A E62A, D99A, K102A, R135A, R136A, R142A, R161A, R198A, K201A −6.36 (± 0.23) 4.4 × 10−7, (2.6 × 10−7–7.4 × 10−7) 25 (± 4)
N4A R135A, R136A, R142A, R161A −6.69 (± 0.14) 2.0 × 10−7, (1.5 × 10−7–2.8 × 10−7) 44 (± 3)

N.A., not applicable.