ABCMdb

ABCC8 p.Cys170Ala

Predicted by SNAP2:	A: N (78%), D: D (59%), E: N (53%), F: N (72%), G: N (61%), H: N (78%), I: N (61%), K: N (61%), L: N (72%), M: N (53%), N: N (57%), P: D (63%), Q: N (61%), R: N (61%), S: N (82%), T: N (72%), V: N (82%), W: N (57%), Y: N (72%),
Predicted by PROVEAN:	A: D, D: N, E: D, F: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, Q: D, R: D, S: D, T: D, V: D, W: D, Y: D,

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Publications
[hide] Transmembrane topology of the sulfonylurea recepto... J Biol Chem. 2001 Nov 2;276(44):41270-8. Epub 2001 Aug 23. Conti LR, Radeke CM, Shyng SL, Vandenberg CA
Transmembrane topology of the sulfonylurea receptor SUR1.
J Biol Chem. 2001 Nov 2;276(44):41270-8. Epub 2001 Aug 23., [PMID:11546780]

Abstract [show]
Sulfonylurea receptors (SURx) are multi-spanning transmembrane proteins of the ATP-binding cassette (ABC) family, which associate with Kir6.x to form ATP-sensitive potassium channels. Two models, with 13-17 transmembrane segments, have been proposed for SURx topologies. Recently, we demonstrated that the amino-terminal region of SUR1 contains 5 transmembrane segments, supporting the 17-transmembrane model. To investigate the topology of the complete full-length SUR1, two strategies were employed. Topology was probed by accessibility of introduced cysteines to a membrane-impermeable biotinylating reagent, biotin maleimide. Amino acid positions 6/26, 99, 159, 337, 567, 1051, and 1274 were accessible, therefore extracellular, whereas many endogenous and some introduced cysteines were inaccessible, thus likely cytoplasmic or intramembrane. These sites correspond to extracellular loops 1-3, 5-6, and 8 and the NH2 terminus, and intracellular loops 3-8 and COOH terminus in the 17-transmembrane model. Immunofluorescence was used to determine accessibility of epitope-tagged SUR1 in intact and permeabilized cells. Epitopes at positions 337 and 1050 (putative external loops 3 and 6) were labeled in intact cells, therefore external, whereas positions 485 and 1119 (putative internal loops 5 and 7) only were accessible after permeabilization and therefore internal. These results are compatible with the 17-transmembrane model with two pairs of transmembrane segments as possible reentrant loops.

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No. Sentence Comment
57 The resulting SUR1AAA construct containing C6S, C26S, C170A, C1051S, and C1057S was referred to as NEC (no external cysteines). Login to comment
55 The resulting SUR1AAA construct containing C6S, C26S, C170A, C1051S, and C1057S was referred to as NEC (no external cysteines). Login to comment