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PMID: 18328253
Loo TW, Clarke DM
Mutational analysis of ABC proteins.
Arch Biochem Biophys. 2008 Aug 1;476(1):51-64. Epub 2008 Mar 5.,
[PubMed]
Sentences
No.
Mutations
Sentence
Comment
127
ABCG2 p.Asp210Asn
X
ABCG2 p.Asp210Asn 18328253:127:115
status:
NEW
view ABCG2 p.Asp210Asn details
In another approach to determine if BCRP functioned as a dimer, inactive mutants were constructed by introducing a
D210N
change in the Walker B motif [44].
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128
ABCG2 p.Asp210Asn
X
ABCG2 p.Asp210Asn 18328253:128:135
status:
NEW
view ABCG2 p.Asp210Asn details
Chimeric BCRP molecules were constructed that contained two wild-type BCRP molecules fused together or a wild-type molecule fused to a
D210N
mutant.
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130
ABCG2 p.Asp210Asn
X
ABCG2 p.Asp210Asn 18328253:130:49
status:
NEW
view ABCG2 p.Asp210Asn details
Expression of the chimeric molecule containing a
D210N
mutation, however, resulted in a dominant-negative phenotype, as the protein was expressed at the cell surface but was not functional.
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313
ABCB1 p.Gly341Cys
X
ABCB1 p.Gly341Cys 18328253:313:63
status:
NEW
view ABCB1 p.Gly341Cys details
ABCB3 p.Val331Cys
X
ABCB3 p.Val331Cys 18328253:313:28
status:
NEW
view ABCB3 p.Val331Cys details
Seven TM6 cysteine mutants (
V331C
, T333C, F335C, S337C, L339C,
G341C
, F343C) were labeled in the presence or absence of AMPPNP or after vanadate trapping of nucleotide.
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315
ABCB1 p.Gly341Cys
X
ABCB1 p.Gly341Cys 18328253:315:63
status:
NEW
view ABCB1 p.Gly341Cys details
ABCC5 p.Phe343Cys
X
ABCC5 p.Phe343Cys 18328253:315:70
status:
NEW
view ABCC5 p.Phe343Cys details
ABCC5 p.Leu339Cys
X
ABCC5 p.Leu339Cys 18328253:315:56
status:
NEW
view ABCC5 p.Leu339Cys details
ABCC5 p.Phe335Cys
X
ABCC5 p.Phe335Cys 18328253:315:42
status:
NEW
view ABCC5 p.Phe335Cys details
ABCC5 p.Ser337Cys
X
ABCC5 p.Ser337Cys 18328253:315:49
status:
NEW
view ABCC5 p.Ser337Cys details
ABCB3 p.Val331Cys
X
ABCB3 p.Val331Cys 18328253:315:28
status:
NEW
view ABCB3 p.Val331Cys details
Seven TM6 cysteine mutants (
V331C
, T333C,
F335C
,
S337C
,
L339C
,
G341C
,
F343C
) were labeled in the presence or absence of AMPÁPNP or after vanadate trapping of nucleotide.
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317
ABCC5 p.Phe343Cys
X
ABCC5 p.Phe343Cys 18328253:317:25
status:
NEW
view ABCC5 p.Phe343Cys details
For example, only mutant
F343C
was significantly labeled with fluorescein maleimide in the absence of nucleotide and labeling was lost in the presence of AMPÁPNP or after vanadate trapping of nucleotide.
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318
ABCB3 p.Val331Cys
X
ABCB3 p.Val331Cys 18328253:318:21
status:
NEW
view ABCB3 p.Val331Cys details
For example, mutants
V331C
and L339C could be labeled in the absence of nucleotide or after vanadate trapping but not in the presence of AMPPNP.
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320
ABCC5 p.Leu339Cys
X
ABCC5 p.Leu339Cys 18328253:320:31
status:
NEW
view ABCC5 p.Leu339Cys details
ABCB3 p.Val331Cys
X
ABCB3 p.Val331Cys 18328253:320:21
status:
NEW
view ABCB3 p.Val331Cys details
For example, mutants
V331C
and
L339C
could be labeled in the absence of nucleotide or after vanadate trapping but not in the presence of AMPÁPNP.
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321
ABCC5 p.Ser337Cys
X
ABCC5 p.Ser337Cys 18328253:321:32
status:
NEW
view ABCC5 p.Ser337Cys details
By contrast, labeling of mutant
S337C
only occurred after vanadate trapping of nucleotide.
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368
ABCB1 p.Ile306Arg
X
ABCB1 p.Ile306Arg 18328253:368:56
status:
NEW
view ABCB1 p.Ile306Arg details
In drug-stimulated ATPase assays, it was found that the
I306R
mutation completely abolished vinblastine-stimulated ATPase activity but had little effect on rhodamine-stimulated ATPase activity [112].
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370
ABCB1 p.Ile306Arg
X
ABCB1 p.Ile306Arg 18328253:370:56
status:
NEW
view ABCB1 p.Ile306Arg details
In drug-stimulated ATPase assays, it was found that the
I306R
mutation completely abolished vinblastine-stimulated ATPase activity but had little effect on rhodamine-stimulated ATPase activity [112].
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372
ABCB1 p.Ile306Arg
X
ABCB1 p.Ile306Arg 18328253:372:15
status:
NEW
view ABCB1 p.Ile306Arg details
The effects of
I306R
mutation on vinblastine interactions were similar in the ATPase and cross-linking assays.
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373
ABCC1 p.Phe728Cys
X
ABCC1 p.Phe728Cys 18328253:373:58
status:
NEW
view ABCC1 p.Phe728Cys details
ABCC5 p.Leu339Cys
X
ABCC5 p.Leu339Cys 18328253:373:52
status:
NEW
view ABCC5 p.Leu339Cys details
Introduction of the I306R(TM5) mutation into mutant
L339C
/
F728C
reduced its apparent affinity for vinblastine more than 60-fold but had little effect on its apparent affinity for rhodamine.
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374
ABCB1 p.Ile306Arg
X
ABCB1 p.Ile306Arg 18328253:374:15
status:
NEW
view ABCB1 p.Ile306Arg details
ABCB1 p.Ile306Arg
X
ABCB1 p.Ile306Arg 18328253:374:33
status:
NEW
view ABCB1 p.Ile306Arg details
ABCB1 p.Ile306Arg
X
ABCB1 p.Ile306Arg 18328253:374:89
status:
NEW
view ABCB1 p.Ile306Arg details
The effects of
I306R
mutation on
vinbl
astine interactions were similar in the ATPase and
cross
-linking assays.
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376
ABCB1 p.Ile306Arg
X
ABCB1 p.Ile306Arg 18328253:376:33
status:
NEW
view ABCB1 p.Ile306Arg details
ABCB1 p.Ile306Arg
X
ABCB1 p.Ile306Arg 18328253:376:89
status:
NEW
view ABCB1 p.Ile306Arg details
ABCC5 p.Phe343Arg
X
ABCC5 p.Phe343Arg 18328253:376:99
status:
NEW
view ABCC5 p.Phe343Arg details
ABCC5 p.Phe343Arg
X
ABCC5 p.Phe343Arg 18328253:376:156
status:
NEW
view ABCC5 p.Phe343Arg details
For example, the L65R, T199R and
I306R
mutations inhibited vinblastine interactions, the
I306R
and
F343R
changes inhibited binding of cyclosporin A and the
F343R
mutation inhibited binding of rhodamine.
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