ABCC1 p.Gln834His
| Predicted by SNAP2: | A: N (72%), C: N (82%), D: N (66%), E: N (87%), F: N (87%), G: N (57%), H: N (97%), I: N (72%), K: N (87%), L: N (66%), M: N (82%), N: N (78%), P: D (59%), R: N (66%), S: N (78%), T: N (66%), V: N (72%), W: N (57%), Y: N (93%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: N, F: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, R: D, S: D, T: D, V: D, W: D, Y: D, |
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[hide] ATP-sensitive potassium channels: a model of heter... Annu Rev Physiol. 1999;61:337-62. Seino S
ATP-sensitive potassium channels: a model of heteromultimeric potassium channel/receptor assemblies.
Annu Rev Physiol. 1999;61:337-62., [PMID:10099692]
Abstract [show]
ATP-sensitive K+ channels (KATP channels) play important roles in many cellular functions by coupling cell metabolism to electrical activity. By cloning members of the novel inwardly rectifying K+ channel subfamily Kir6.0 (Kir6.1 and Kir6.2) and the receptors for sulfonylureas (SUR1 and SUR2), researchers have clarified the molecular structure of KATP channels. KATP channels comprise two subunits: a Kir6.0 subfamily subunit, which is a member of the inwardly rectifying K+ channel family; and a SUR subunit, which is a member of the ATP-binding cassette (ABC) protein superfamily. KATP channels are the first example of a heteromultimeric complex assembled with a K+ channel and a receptor that are structurally unrelated to each other. Since 1995, molecular biological and molecular genetic studies of KATP channels have provided insights into the structure-function relationships, molecular regulation, and pathophysiological roles of KATP channels.
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No. Sentence Comment
205 Mutations in the linker region between the Walker A motif and the Walker B motif of NBF-1 (G827D, G827R, and Q834H), the equivalent mutations in NBF-2 (G1479D, G1479R, G1485D, G1485R, Q1486H), or the mutation of Walker B motif of NBF-2 (D1506A) do not abolish channel inhibition by ATP (105).
X
ABCC1 p.Gln834His 10099692:205:109
status: NEW211 Mutations in the linker region and the Walker B motif of NBF-2 (G1479D, G1479R, G1485D, G1485R, Q1486H, and D1506A) abolish channel activation by diazoxide, and mutations in the linker region of NBF-1 (G827D, G827R, and Q834H) alter the kinetics of diazoxide activation (106).
X
ABCC1 p.Gln834His 10099692:211:220
status: NEW