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PMID: 7515047
Akabas MH, Kaufmann C, Cook TA, Archdeacon P
Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator.
J Biol Chem. 1994 May 27;269(21):14865-8.,
[PubMed]
Sentences
No.
Mutations
Sentence
Comment
15
ABCC7 p.Arg347Glu
X
ABCC7 p.Arg347Glu 7515047:15:50
status:
NEW
view ABCC7 p.Arg347Glu details
ABCC7 p.Lys335Glu
X
ABCC7 p.Lys335Glu 7515047:15:38
status:
NEW
view ABCC7 p.Lys335Glu details
ABCC7 p.Lys95Asp
X
ABCC7 p.Lys95Asp 7515047:15:12
status:
NEW
view ABCC7 p.Lys95Asp details
Mutation of
Lys-95 to Asp
, in M1, and
Lys-335 and Arg-347 to Glu
, in M6, altered the permeability andlor conductance ratios for halides (6).
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16
ABCC7 p.Arg117His
X
ABCC7 p.Arg117His 7515047:16:54
status:
NEW
view ABCC7 p.Arg117His details
ABCC7 p.Arg334Trp
X
ABCC7 p.Arg334Trp 7515047:16:61
status:
NEW
view ABCC7 p.Arg334Trp details
ABCC7 p.Arg347Pro
X
ABCC7 p.Arg347Pro 7515047:16:72
status:
NEW
view ABCC7 p.Arg347Pro details
Three mutationsassociated with mild clinical disease,
R117H
,
R334W
, and
R347P
,displayed altered single-channel properties (ll), but the structural basisof the functional changes is unknown.
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18
ABCC7 p.Arg347His
X
ABCC7 p.Arg347His 7515047:18:12
status:
NEW
view ABCC7 p.Arg347His details
Mutation of
Arg-347 to His
resulted in theability to eliminate themultiple ion occupancy effects by changing the pH of the intracellular solution, presumablyby titrating the stateof protonation of the histidine.
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69
ABCC7 p.Lys95Cys
X
ABCC7 p.Lys95Cys 7515047:69:131
status:
NEW
view ABCC7 p.Lys95Cys details
ABCC7 p.Gly91Cys
X
ABCC7 p.Gly91Cys 7515047:69:125
status:
NEW
view ABCC7 p.Gly91Cys details
ABCC7 p.Gln98Cys
X
ABCC7 p.Gln98Cys 7515047:69:141
status:
NEW
view ABCC7 p.Gln98Cys details
Application of the MTS reagents irreversibly alteredthe CFTR-induced currents of three of the cysteine substitution mutants,
G91C
,
K95C
, and
Q98C
.
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71
ABCC7 p.Gly91Cys
X
ABCC7 p.Gly91Cys 7515047:71:76
status:
NEW
view ABCC7 p.Gly91Cys details
2B and 3A).Application of MTSEA`for 1min irreversibly inhibited the mutants
G91C
by 43 * 6% (n = 5) (Figs.
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72
ABCC7 p.Lys95Cys
X
ABCC7 p.Lys95Cys 7515047:72:80
status:
NEW
view ABCC7 p.Lys95Cys details
ABCC7 p.Gln98Cys
X
ABCC7 p.Gln98Cys 7515047:72:15
status:
NEW
view ABCC7 p.Gln98Cys details
20 and 3C) and
Q98C
by 32 2 4% (n= 9) and potentiated the current of the mutant
K95C
by 108 2 22%(n = 4) (Figs.
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75
ABCC7 p.Lys95Cys
X
ABCC7 p.Lys95Cys 7515047:75:50
status:
NEW
view ABCC7 p.Lys95Cys details
ABCC7 p.Gly91Cys
X
ABCC7 p.Gly91Cys 7515047:75:59
status:
NEW
view ABCC7 p.Gly91Cys details
The anionic reagent, MTSES-, had no effect on the
K95C
and
G91C
mutants (Fig. 3,A andB).To determine whether thelack of effect was due to inability to react with Cys-95 or lack of effect followingreaction, we sequentially applied MTSES- and MTSEA+;MTSES- did not prevent the potentiationof the current by MTSEA+(data notshown).
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82
ABCC7 p.Lys95Cys
X
ABCC7 p.Lys95Cys 7515047:82:89
status:
NEW
view ABCC7 p.Lys95Cys details
The effect ofthe MTS reagentson wild typeCFTR and on thethreechannel-liningmutants GSlC,
K95C
,and QSSC.
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86
ABCC7 p.Lys95Cys
X
ABCC7 p.Lys95Cys 7515047:86:63
status:
NEW
view ABCC7 p.Lys95Cys details
ABCC7 p.Gly91Cys
X
ABCC7 p.Gly91Cys 7515047:86:72
status:
NEW
view ABCC7 p.Gly91Cys details
ABCC7 p.Gln98Cys
X
ABCC7 p.Gln98Cys 7515047:86:55
status:
NEW
view ABCC7 p.Gln98Cys details
A and C are from oocytesinjectedwith wild type CFTR B,
Q98C
; D,
K95C
; E,
G91C
.
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97
ABCC7 p.Lys95Cys
X
ABCC7 p.Lys95Cys 7515047:97:39
status:
NEW
view ABCC7 p.Lys95Cys details
The application ofMTSEA' to the mutant
K95C
increased the CFTR-induced current.
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101
ABCC7 p.Lys95Cys
X
ABCC7 p.Lys95Cys 7515047:101:21
status:
NEW
view ABCC7 p.Lys95Cys details
ABCC7 p.Lys95Cys
X
ABCC7 p.Lys95Cys 7515047:101:30
status:
NEW
view ABCC7 p.Lys95Cys details
1 MINMTS-EA, 8 MIN C
K95C
5 D
K95C
5 I -50 0 50 100 150-50 0 50 100 150 CHANGEINCURRENT (X) FIG.3.
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110
ABCC7 p.Lys95Cys
X
ABCC7 p.Lys95Cys 7515047:110:69
status:
NEW
view ABCC7 p.Lys95Cys details
ABCC7 p.Gly91Cys
X
ABCC7 p.Gly91Cys 7515047:110:64
status:
NEW
view ABCC7 p.Gly91Cys details
ABCC7 p.Gln98Cys
X
ABCC7 p.Gln98Cys 7515047:110:78
status:
NEW
view ABCC7 p.Gln98Cys details
Based on the accessibility of the cysteine-substitution mutants
G91C
,
K95C
and
Q98C
to the MTS reagents, we infer that the side chains of the corresponding wild type residues, Gly-91,Lys-95, and Gln-98, line the channel ofCFTR.
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122
ABCC7 p.Gly91Arg
X
ABCC7 p.Gly91Arg 7515047:122:200
status:
NEW
view ABCC7 p.Gly91Arg details
ABCC7 p.Gly91Cys
X
ABCC7 p.Gly91Cys 7515047:122:167
status:
NEW
view ABCC7 p.Gly91Cys details
Although the Arg side chain is somewhat larger than theside chain of Cys modified by MTSEA', the reduction in whole cell current we observed following modification of
G91C
by MTSEA' suggests that the
G91R
mutant will have altered single-channel properties.
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123
ABCC7 p.Lys95Asp
X
ABCC7 p.Lys95Asp 7515047:123:132
status:
NEW
view ABCC7 p.Lys95Asp details
Effects on single-channel properties have been observed with other missense mutations associated with mild disease (11).Mutation of
Lys-95 to Asp
altered the relative anionper- meability sequence of the channel, although no evidence was presented that Lys-95 actually faced the channel lumen (6).
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