ABCC7 p.Val232Gln
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PMID: 24412276
[PubMed]
Loo TW et al: "The cystic fibrosis V232D mutation inhibits CFTR maturation by disrupting a hydrophobic pocket rather than formation of aberrant interhelical hydrogen bonds."
No.
Sentence
Comment
89
Further evidence for hydrogen bond formation was that the V232Q/Q207D mutant (reversal of the Gln and Asp positions) also migrated faster on SDS-PAGE gels [24].
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ABCC7 p.Val232Gln 24412276:89:58
status: NEW127 Inhibition of CFTR maturation correlates with the polarity of a Val232 mutation If V232D inhibits CFTR maturation by forming a non-native hydrogen bond with Gln207, then it would be expected that V232N and V232Q mutations would also severely inhibit maturation since asparagine and glutamine are structurally similar to aspartate and their amide groups can accept or donate two hydrogen bonds.
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ABCC7 p.Val232Gln 24412276:127:206
status: NEW128 Accordingly, mutants V232N and V232Q were constructed.
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ABCC7 p.Val232Gln 24412276:128:31
status: NEW131 By contrast, the amount of mature protein was about 20-fold higher (about 40%) for mutants V232N and V232Q compared to V232D or V232E (Fig. 3).
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ABCC7 p.Val232Gln 24412276:131:101
status: NEW137 The V232N and V232Q mutations modestly reduced the yield of mature CFTR by about half (80% for wild-type CFTR compared to about 40% for mutants V232N or V232Q) (Fig. 3).
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ABCC7 p.Val232Gln 24412276:137:14
status: NEWX
ABCC7 p.Val232Gln 24412276:137:153
status: NEW138 The V232N and V232Q mutations may have reduced maturation because of a change in polarity or because introduction of a larger side chain caused steric effects that disrupted packing of the TM segments.
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ABCC7 p.Val232Gln 24412276:138:14
status: NEW