ABCC8 p.Trp232Ala
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PMID: 15561897
[PubMed]
Bryan J et al: "Toward linking structure with function in ATP-sensitive K+ channels."
No.
Sentence
Comment
146
Substitution of Trp232 with alanine results in loss of affinity labeling, whereas replacement with cysteine retains labeling.
X
ABCC8 p.Trp232Ala 15561897:146:16
status: NEW162 Results for the wild-type (WT) control, the Tyr230Ala (Y230A), and Trp231Ala (W232A) substitutions are shown.
X
ABCC8 p.Trp232Ala 15561897:162:78
status: NEW
PMID: 17110465
[PubMed]
Vila-Carriles WH et al: "Defining a binding pocket for sulfonylureas in ATP-sensitive potassium channels."
No.
Sentence
Comment
104
The graph shows a decrease in photoaffinity labeling for SUR1 Y230A and W232A (Fig. 3C).
X
ABCC8 p.Trp232Ala 17110465:104:72
status: NEW126 The data are plotted as the ratio of label-toprotein in arbitrary units Ϯ sd. the SUR1, Y230A, and W232A substitutions.
X
ABCC8 p.Trp232Ala 17110465:126:106
status: NEWX
ABCC8 p.Trp232Ala 17110465:126:109
status: NEW127 Both SUR1 and KIR6.2 in KATP channels are affinity-labeled by [125 I]-azido-glibenclamide and coexpression of SUR1, Y230A, and W232A with KIR6.2 resulted in labeling of the KIR (data not shown) and also in an increase of the mutant SUR1 labeling (Fig. 6).
X
ABCC8 p.Trp232Ala 17110465:127:127
status: NEW129 When SUR1 Y230A, and W232A were coexpressed with ⌵⌬33KIR6.2, a KIR6.2 construct that does not photolabel, none of the SUR1 mutants labeled (Fig. 6), indicating that the KIR6.2 N terminus play a role in the sulfonylurea binding pocket.
X
ABCC8 p.Trp232Ala 17110465:129:21
status: NEW184 When SUR1 and the SUR1 alanine point mutations Y230A and W232A were coexpressed with KIR, this resulted in an increase in [125 I]-azido-glibenclamide labeling and KIR cophotolabeling, consistent with KIR forming part of the B site.
X
ABCC8 p.Trp232Ala 17110465:184:57
status: NEW189 Wild-type SUR1, SUR1, Y230A, and W232A were expressed or coexpressed with either KIR6.2 or N⌬33KIR6.2 in COSm6 cells.
X
ABCC8 p.Trp232Ala 17110465:189:33
status: NEW192 However, coexpression of SUR1, Y230A, and W232A with N⌬33KIR6.2 did not increase labeling of SUR1 or the mutants.
X
ABCC8 p.Trp232Ala 17110465:192:42
status: NEW103 The graph shows a decrease in photoaffinity labeling for SUR1 Y230A and W232A (Fig. 3C).
X
ABCC8 p.Trp232Ala 17110465:103:72
status: NEW125 The data are plotted as the ratio of label-to- protein in arbitrary units afe; sd. the SUR1, Y230A, and W232A substitutions.
X
ABCC8 p.Trp232Ala 17110465:125:109
status: NEW128 When SUR1 Y230A, and W232A were coexpressed with टèc;33KIR6.2, a KIR6.2 construct that does not photolabel, none of the SUR1 mutants labeled (Fig. 6), indicating that the KIR6.2 N terminus play a role in the sulfonylurea binding pocket.
X
ABCC8 p.Trp232Ala 17110465:128:21
status: NEW183 When SUR1 and the SUR1 alanine point mutations Y230A and W232A were coexpressed with KIR, this resulted in an increase in [125 I]-azido-glibenclamide labeling and KIR cophotolabeling, consistent with KIR forming part of the B site.
X
ABCC8 p.Trp232Ala 17110465:183:57
status: NEW188 Wild-type SUR1, SUR1, Y230A, and W232A were expressed or coexpressed with either KIR6.2 or Nèc;33KIR6.2 in COSm6 cells.
X
ABCC8 p.Trp232Ala 17110465:188:33
status: NEW191 However, coexpression of SUR1, Y230A, and W232A with Nèc;33KIR6.2 did not increase labeling of SUR1 or the mutants.
X
ABCC8 p.Trp232Ala 17110465:191:42
status: NEW