ABCC8 p.Asp860Ala
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PMID: 16442101
[PubMed]
Frelet A et al: "Insight in eukaryotic ABC transporter function by mutation analysis."
No.
Sentence
Comment
316
[143] SUR1 D860A D860A not activated by MgADP in either presence or absence of MgATP.
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ABCC8 p.Asp860Ala 16442101:316:11
status: NEWX
ABCC8 p.Asp860Ala 16442101:316:17
status: NEW
PMID: 15561899
[PubMed]
Campbell JD et al: "Identification of a functionally important negatively charged residue within the second catalytic site of the SUR1 nucleotide-binding domains."
No.
Sentence
Comment
5
We tested this prediction experimentally and found that, unlike wild-type channels, channels containing the SUR1-D860A mutation were not activated by MgADP in either the presence or absence of MgATP.
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ABCC8 p.Asp860Ala 15561899:5:113
status: NEW77 Effects of the D860A mutation on Mg nucleotide activation.
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ABCC8 p.Asp860Ala 15561899:77:15
status: NEW82 Addition of 100 mol/l MgATP produced a greater block of Kir6.2/SUR1-D860A channels than of wild-type channels: 95 Ϯ 1% (n ϭ 3) compared with 85 Ϯ 5% (n ϭ 3) (Fig. 2).
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ABCC8 p.Asp860Ala 15561899:82:76
status: NEW84 MgADP was unable to stimulate the activity of channels carrying the D860A mutation in the presence of ATP, in contrast to wild-type channels (Fig. 2).
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ABCC8 p.Asp860Ala 15561899:84:68
status: NEW88 A: Macroscopic currents recorded from oocytes coexpressing Kir6.2 and either SUR1, or SUR2B- D860A in response to a series of voltage ramps from -110 to ؉100 mV. 100 mol/l ADP and 100 mol/l ATP were added to the intracellular solution as indicated by the bars.
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ABCC8 p.Asp860Ala 15561899:88:93
status: NEW90 B: Mean KATP conductance recorded in response to 100 mol/l ADP, 100 mol/l ATP, or 100 mol/l ADP ؉ 100 mol/l ATP in patches excised from oocytes coexpressing Kir6.2 and either wild-type SUR1 (Ⅺ) or SUR1-D860A (f).
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ABCC8 p.Asp860Ala 15561899:90:247
status: NEW104 We ran four simulations: the wild-type model with 1) ATP docked at both NBDs, or 2) ATP docked at NBD1 and ADP docked at NBD2, and 3, 4) the equivalent simulations of the D860A mutant.
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ABCC8 p.Asp860Ala 15561899:104:171
status: NEW106 Furthermore, the D860A simulations demonstrate that removal of the negatively charged aspartate disrupts the interaction of R1379 with nucleotide; in contrast to the wild-type simulations, R1379 more strongly interacts with the ATP than with ADP.
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ABCC8 p.Asp860Ala 15561899:106:17
status: NEW