ABCC7 p.Ser495Pro
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PMID: 25083918
[PubMed]
He L et al: "Restoration of NBD1 thermal stability is necessary and sufficient to correct F508 CFTR folding and assembly."
No.
Sentence
Comment
72
2PT, S492P/ A534P/I539T; 3PT, 2PT + S495P.
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ABCC7 p.Ser495Pro 25083918:72:36
status: NEW93 In addition to the S492P substitution found in three non-mammalian species that are relatively insensitive to the destabilizing influence of the ƊF508 mutation [13], we also included a second Q-loop proline substitution, S495P present in shark CFTR.
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ABCC7 p.Ser495Pro 25083918:93:226
status: NEW97 The S495P substitution alone in the isolated NBD1 of human CFTR caused the largest increase in Tm (5.99 &#b1; 0.33 &#b0;C) of any single change tested (Fig. 2a, lower panel).
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ABCC7 p.Ser495Pro 25083918:97:4
status: NEW98 Therefore, we compared the effect of S495P with that of other NBD1 stabilizing mutations on the maturation of ƊF508 CFTR.
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ABCC7 p.Ser495Pro 25083918:98:37
status: NEW99 As shown in Fig. 2b, the S495P substitution in ƊF508 CFTR resulted in substantial maturation.
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ABCC7 p.Ser495Pro 25083918:99:25
status: NEW101 Combination of I539T with S495P, however, did cause a further increase in maturation and the effects of the two proline substitutions also were additive.
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ABCC7 p.Ser495Pro 25083918:101:26
status: NEW179 Strikingly, the introduction of a proline residue at position 495 (S495P) in the Q-loop was found to cause the largest increase in the domain Tm and have the strongest restorative effect on maturation of the full-length protein of any single NBD1 second-site change and its influence was additive with others (Fig. 2).
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ABCC7 p.Ser495Pro 25083918:179:67
status: NEW191 As demonstrated in the current work the S495P mutation, two residues C-terminal of the Q-loop glutamine have the greatest impact.
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ABCC7 p.Ser495Pro 25083918:191:40
status: NEW
PMID: 26149808
[PubMed]
Chong PA et al: "Deletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization."
No.
Sentence
Comment
386
Other published Q-loop segment suppressor mutations such as S492P and S495P (21, 29) are also likely to modulate NBD dimerization.
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ABCC7 p.Ser495Pro 26149808:386:70
status: NEW