ABCC7 p.Phe508Asn
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PMID: 15619636
[PubMed]
Thibodeau PH et al: "Side chain and backbone contributions of Phe508 to CFTR folding."
No.
Sentence
Comment
91
Band C levels in F508A, F508G, F508L and F508V as well as the polar amino acid substitutions F508S, F508T, F508N and F508Q were evident, but substantially reduced relative to wild-type band C levels.
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ABCC7 p.Phe508Asn 15619636:91:107
status: NEW113 W ild type ∆∆F508 F508 F508D F508K F508E F508R F508H F508S F508T F508N F508Q C B Charged Polar F508A F508C F508I F508L ∆F508 F508 W ild type C B F508W F508Y F508G F508P Hydrophobic F508M F508V ̅̆ ̆ ̅ Figure 3 Maturation of full-length CFTR mutants.
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ABCC7 p.Phe508Asn 15619636:113:79
status: NEW
PMID: 22265408
[PubMed]
Rabeh WM et al: "Correction of both NBD1 energetics and domain interface is required to restore DeltaF508 CFTR folding and function."
No.
Sentence
Comment
69
These results in concert with the effect of F508E, F508R, F508G, F508S, F508D, and F508N mutations revealed that the CD4T-NBD1 PM density was proportional to the domain stability if the NBD1 Tm was >38 C (Figures 3D and S4D).
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ABCC7 p.Phe508Asn 22265408:69:83
status: NEW121 Missense mutations of F508 are depicted by colored squares (-), and F508N-3S and -R are indicated by solid triangle (:).
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ABCC7 p.Phe508Asn 22265408:121:68
status: NEW125 (2) Although certain combinations of F508N and R or S mutations conferred thermodynamic and kinetic stability comparable with or exceeding that of the WT NBD1-1S (e.g., F508N-R; DG0 = À5.1 ± 0.1 kcal/mol, Tm z47 C and ku H20 = 0.16 10À3 secÀ1 ; Figure S5), they failed to restore WT-like folding and expression of the DF508 CFTR (Figures 5A and 5B).
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ABCC7 p.Phe508Asn 22265408:125:37
status: NEWX
ABCC7 p.Phe508Asn 22265408:125:169
status: NEW122 Missense mutations of F508 are depicted by colored squares (-), and F508N-3S and -R are indicated by solid triangle (:).
X
ABCC7 p.Phe508Asn 22265408:122:68
status: NEW126 (2) Although certain combinations of F508N and R or S mutations conferred thermodynamic and kinetic stability comparable with or exceeding that of the WT NBD1-1S (e.g., F508N-R; DG0 = 5.1 &#b1; 0.1 kcal/mol, Tm z47 C and ku H20 = 0.16 103 sec1 ; Figure S5), they failed to restore WT-like folding and expression of the DF508 CFTR (Figures 5A and 5B).
X
ABCC7 p.Phe508Asn 22265408:126:37
status: NEWX
ABCC7 p.Phe508Asn 22265408:126:169
status: NEW