ABCC7 p.Gly1247Asp
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PMID: 9920885
[PubMed]
Lee MG et al: "Regulation of Cl-/ HCO3- exchange by cystic fibrosis transmembrane conductance regulator expressed in NIH 3T3 and HEK 293 cells."
No.
Sentence
Comment
52
The mutagenesis primers were as follows: P205S primer, 5Ј-CGT GTG GAT CGC TTC TTT GCA AGT GGC-3Ј; W846term, 5Ј-GAG CAT ACC AGC AGT GAC TAC ATA GAA CAC ATA CCT TCG ATA TAT TAC-3Ј; G1247D/G1249E, 5Ј-GTG GGC CTC TTG GGA AGA ACT GAT TCA GAG AAG AGT ACT TTG TTA TCA GC-3Ј; K1250M, 5Ј-CTT GGG AAG AAC TGG ATC AGG GAT GAG TAC TTT GTT ATC AGC-3Ј; D1370N, 5Ј-GTA AGG CGA AGA TCT TGC TGC TTA ATG AAC CCA GTG CTC ATT TGG ATC-3Ј.
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ABCC7 p.Gly1247Asp 9920885:52:203
status: NEW163 Fig. 6 (i-k) shows the plasma membrane localization of K1250M CFTR, D1370N CFTR, and the double mutant G1247D/ G1249E CFTR, respectively.
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ABCC7 p.Gly1247Asp 9920885:163:103
status: NEW239 For example, the G1247D/G1249E CFTR double mutant was reported to have no Cl-channel activity (32), was expressed in the plasma membrane (Fig. 6k), and had no effect on AE activity (Fig. 12a).
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ABCC7 p.Gly1247Asp 9920885:239:17
status: NEW264 The G1247D/G1249E double mutant was expressed in the plasma membrane but had no effect on AE activity (a).
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ABCC7 p.Gly1247Asp 9920885:264:4
status: NEW
PMID: 9922377
[PubMed]
Gadsby DC et al: "Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis."
No.
Sentence
Comment
563
Second, mutant G1247D/G1249E CFTRphorylation status) of the closings are expected to be rate limited by ATP hydrolysis.
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ABCC7 p.Gly1247Asp 9922377:563:15
status: NEW
No.
Sentence
Comment
331
Mutations predicted to abolish nucleotide binding at NBD2, a G1247D/G1249E double mutant, exhibit low Po because of extended closed times and only brief openings (to O1 only), which are independent of ATP (150).
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ABCC7 p.Gly1247Asp 9558482:331:61
status: NEW
PMID: 7543023
[PubMed]
Gunderson KL et al: "Conformational states of CFTR associated with channel gating: the role ATP binding and hydrolysis."
No.
Sentence
Comment
117
The effect of this double mutation, G1247D and G1249E, is to introduce negative charge into the P loop, which should severely attenuate nucleotide binding to NBF2.
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ABCC7 p.Gly1247Asp 7543023:117:36
status: NEW121 The simplest interpretation of these data is that ATP binding ConformationalStatesof CFTR 09 08 07 06 Oo 05 040.3 * 32 wildtype K464A K1250A G1247D/ D1370N 01249E 6~se' B 2500 20O0 5 1500 1OO0 500 o~ 0 w[Id{ype K464A K1250A C1247D/ Ol 370N G1249E Figure5.
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ABCC7 p.Gly1247Asp 7543023:121:143
status: NEW178 The proposal that ATP binding to NBF2 opens the channel to the O1 state is supported by the virtual absence of ATP-dependent openings in the G1247D, G1249E P loop mutant.
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ABCC7 p.Gly1247Asp 7543023:178:141
status: NEW118 The effect of this double mutation, G1247D and G1249E, is to introduce negative charge into the P loop, which should severely attenuate nucleotide binding to NBF2.
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ABCC7 p.Gly1247Asp 7543023:118:36
status: NEW122 The simplest interpretation of these data is that ATP binding ConformationalStatesof CFTR 09 08 07 06 Oo 05 040.3 * 32 wildtype K464A K1250A G1247D/ D1370N 01249E 6~se' B 2500 20O0 5 1500 1OO0 500 o ~ 0 w[Id{ype K464A K1250A C1247D/ Ol 370N G1249E Figure5.
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ABCC7 p.Gly1247Asp 7543023:122:143
status: NEW179 The proposal that ATP binding to NBF2 opens the channel to the O1 state is supported by the virtual absence of ATP-dependent openings in the G1247D, G1249E P loop mutant.
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ABCC7 p.Gly1247Asp 7543023:179:141
status: NEW