ABCC8 p.Asp18Ala

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PMID: 9738007 [PubMed] Gasparini S et al: "Delineation of the functional site of alpha-dendrotoxin. The functional topographies of dendrotoxins are different but share a conserved core with those of other Kv1 potassium channel-blocking toxins."
No. Sentence Comment
134 The other substitutions (P2A, H10A, R11A, R15A, Y17A, and D18A) and the previously described mutation D12N (32) did not significantly reduce the affinity.
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ABCC8 p.Asp18Ala 9738007:134:58
status: NEW
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193 The spectra were recorded at 20 °C in 0.1-cm cuvettes, with a protein concentration of 5-10 ␮M. TABLE I Affinity of ␣DTX analogs determined by their ability to compete with [125 I]␣DTX for binding to rat brain synaptosomal membranes ␣DTX Ki a Ki analog/Ki WTb pM WT 4 Ϯ 1 1 P2A 10.6 Ϯ 1.1 2.9 Ϯ 1.0 R3A 28.5 Ϯ 4.6 7.9 Ϯ 3.1 R4A 38 Ϯ 12 11 Ϯ 5.75 K5A 5800 Ϯ 700 1594 Ϯ 574 K5Orn 471 Ϯ 42 128 Ϯ 43 K5Nle 5700 Ϯ 400 1547 Ϯ 487 L6A 43.4 Ϯ 12 12.4 Ϯ 6.1 I8A 118 Ϯ 26 33.2 Ϯ 14.8 L9A 4160 Ϯ 900 1170 Ϯ 518 H10A 1.6 Ϯ 0.2 0.45 Ϯ 0.15 R11A 3.0 Ϯ 0.1 0.8 Ϯ 0.2 R15A 4.6 Ϯ 0.1 1.22 Ϯ 0.33 Y17A 3.7 Ϯ 0.1 1.0 Ϯ 0.27 D18A 3.4 Ϯ 0.1 0.91 Ϯ 0.25 K19A 2.3 Ϯ 0.1 0.63 Ϯ 0.17 Q27A 2.9 Ϯ 0.1 0.78 Ϯ 0.21 Q31A 3.65 Ϯ 0.05 0.98 Ϯ 0.26 E33A 5.3 Ϯ 0.05 1.42 Ϯ 0.37 R34A 7.1 Ϯ 0.1 1.9 Ϯ 0.5 D36A 4.85 Ϯ 0.1 1.30 Ϯ 0.35 S38A 23.5 Ϯ 6.5 6.64 Ϯ 3.24 S44A 6.7 Ϯ 0.1 1.8 Ϯ 0.45 R46A 562 Ϯ 152 160 Ϯ 78 K48A 2.8 Ϯ 0.05 0.75 Ϯ 0.2 E51A 3.65 Ϯ 0.05 0.98 Ϯ 0.26 R54A 5.4 Ϯ 0.05 1.44 Ϯ 0.38 R55A 4.0 Ϯ 0.21 1.08 Ϯ 0.3 I58A 3.45 Ϯ 0.25 1.27 Ϯ 0.63 a Ki Ϯ S.E. values are calculated from competition experiments as described in the legend of Fig. 5. b WT, wild type.
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ABCC8 p.Asp18Ala 9738007:193:800
status: NEW
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