ABCC8 p.Arg388Cys
| Predicted by SNAP2: | A: D (85%), C: D (85%), D: D (95%), E: D (91%), F: D (91%), G: D (85%), H: D (85%), I: D (85%), K: N (61%), L: D (91%), M: D (85%), N: D (91%), P: D (91%), Q: D (75%), S: D (80%), T: D (85%), V: D (85%), W: D (91%), Y: D (91%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: D, K: N, L: D, M: D, N: D, P: D, Q: D, S: D, T: D, V: D, W: D, Y: D, |
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[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
166 Several of the mutations (A161C, R388C, P1162C, and R1300C) produced SUR1 proteins that did not show a complex glycosylated form, and these were not evaluated further.
X
ABCC8 p.Arg388Cys 11546780:166:33
status: NEW165 Several of the mutations (A161C, R388C, P1162C, and R1300C) produced SUR1 proteins that did not show a complex glycosylated form, and these were not evaluated further.
X
ABCC8 p.Arg388Cys 11546780:165:33
status: NEW