ABCC8 p.Thr99Cys
| Predicted by SNAP2: | A: N (78%), C: N (72%), D: N (61%), E: N (61%), F: N (78%), G: N (72%), H: N (87%), I: N (78%), K: N (61%), L: N (87%), M: N (87%), N: N (93%), P: N (72%), Q: N (78%), R: N (78%), S: N (97%), V: N (82%), W: N (57%), Y: N (87%), |
| Predicted by PROVEAN: | A: N, C: D, D: N, E: N, F: N, G: D, H: N, I: N, K: N, L: N, M: N, N: N, P: D, Q: N, R: N, S: N, V: N, W: D, Y: N, |
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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
58 NEC was subjected to PCR mutagenesis to individually introduce cysteines at each putative external loop (T99C, K337C, Y454C, K567C, T1161C, S1186C, and R1274C).
X
ABCC8 p.Thr99Cys 11546780:58:105
status: NEW56 NEC was subjected to PCR mutagenesis to individually introduce cysteines at each putative external loop (T99C, K337C, Y454C, K567C, T1161C, S1186C, and R1274C).
X
ABCC8 p.Thr99Cys 11546780:56:105
status: NEW