ABCB1 p.Val331Ala
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PMID: 9891078
[PubMed]
Zhou Y et al: "Studies of human MDR1-MDR2 chimeras demonstrate the functional exchangeability of a major transmembrane segment of the multidrug transporter and phosphatidylcholine flippase."
No.
Sentence
Comment
49
MDR1NAM was created by introducing mutations Q330N, V331A, and L332M into MDR1 by PCR mutagenesis.
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ABCB1 p.Val331Ala 9891078:49:52
status: NEW169 To confirm the significance of Q330, V331, and L332 in TM6, we generated a MDR1 mutant containing the mutations Q330N, V331A, and L332M.
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ABCB1 p.Val331Ala 9891078:169:119
status: NEW226 One is that the substitutions Q330N, V331A, and L332M in MDR1 significantly decreased overall MDR1 multidrug transporter activity.
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ABCB1 p.Val331Ala 9891078:226:37
status: NEW241 Thus, the triple mutation Q330N, V331A, and L332M appeared to have a synergistic effect.
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ABCB1 p.Val331Ala 9891078:241:33
status: NEW262 Since the UIC2 epitope depends on a particular P-gp conformation (24), the decreased level of UIC2 recognition may indicate a conformational change in MDR1 caused by mutations Q330N, V331A, and L332M.
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ABCB1 p.Val331Ala 9891078:262:183
status: NEW
PMID: 10375401
[PubMed]
Zhou Y et al: "The extracellular loop between TM5 and TM6 of P-glycoprotein is required for reactivity with monoclonal antibody UIC2."
No.
Sentence
Comment
66
Those substitutions are T318S, L322I, G324K, S327T, Q330N, V331A, and L332M (Fig. 1).
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ABCB1 p.Val331Ala 10375401:66:59
status: NEW79 This possibility was examined by testing the UIC2 reactivity of a P-gp mutant, MDR1/ MDR2(330-332), which carried substitutions Q330N, V331A, and L332M in TM6.
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ABCB1 p.Val331Ala 10375401:79:135
status: NEW84 However, in the presence of cyclosporin A, cells expressing MDR1/MDR2(330-332) displayed a number of UIC2 binding sites more similar to cells expressing wild-type P-gp, indicating that the triple mutation (Q330N, V331A, and L332M) in TM6 did not directly affect the affinity of UIC2 for its epitope (Fig. 4).
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ABCB1 p.Val331Ala 10375401:84:213
status: NEW115 Since the substitutions T318S, L322I, G324K, and S327T had little effect on either MRK-16 labeling or multidrug transporter activity, it is less likely that these mutations produce any major changes in P-gp structure.
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ABCB1 p.Val331Ala 10375401:115:75
status: NEW116 UIC2 Reactivity Is Sensitive to Mutations in TM6 A triple mutation, Q330N, V331A, and L332M, in TM6 decreased overall multidrug transporter activity FIG. 3. FACS analysis of cell surface expression of MDR1 and MDR1/MDR2(330-332) using MRK-16 and UIC2.
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ABCB1 p.Val331Ala 10375401:116:75
status: NEW78 This possibility was examined by testing the UIC2 reactivity of a P-gp mutant, MDR1/ MDR2(330-332), which carried substitutions Q330N, V331A, and L332M in TM6.
X
ABCB1 p.Val331Ala 10375401:78:135
status: NEW83 However, in the presence of cyclosporin A, cells expressing MDR1/MDR2(330-332) displayed a number of UIC2 binding sites more similar to cells expressing wild-type P-gp, indicating that the triple mutation (Q330N, V331A, and L332M) in TM6 did not directly affect the affinity of UIC2 for its epitope (Fig. 4).
X
ABCB1 p.Val331Ala 10375401:83:213
status: NEW