ABCC7 p.Gly551Glu
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 21421917
[PubMed]
Balch WE et al: "Emergent properties of proteostasis in managing cystic fibrosis."
No.
Sentence
Comment
47
The G551E and G1349D mutants (purple) are folded and traffic normally to cell surface.
X
ABCC7 p.Gly551Glu 21421917:47:4
status: NEW49 The G551E and G1349D vCFTR only require a potentiator to open the channel and restore function.
X
ABCC7 p.Gly551Glu 21421917:49:4
status: NEW
PMID: 25225552
[PubMed]
Lin WY et al: "A single amino acid substitution in CFTR converts ATP to an inhibitory ligand."
No.
Sentence
Comment
21
G551E, but not G551K or G551S, exhibits a similar phenotype, indicating that electrostatic repulsion between the negatively charged side chain of aspartate and the &#e067;-phosphate of ATP accounts for the observed mutational effects.
X
ABCC7 p.Gly551Glu 25225552:21:0
status: NEW32 Because this inhibitory effect is observed also in G551E, but not in G551K or G551S, a basic chemical mechanism of an electrostatic repulsion between the negatively charged side chain of 551D/E and the &#e067;-phosphate of ATP in shaping the observed mutational effects is proposed.
X
ABCC7 p.Gly551Glu 25225552:32:51
status: NEW164 In contrast, G551E-CFTR channels behave just like G551D-CFTR (Fig. 6 C), suggesting that an anionic side chain at residue 551 is required to confer this inhibitory action to site 2.
X
ABCC7 p.Gly551Glu 25225552:164:13
status: NEW191 (A-C) Responses to ATP withdrawal in different G551 mutants: G551S (A), G551K (B), and G551E (C).
X
ABCC7 p.Gly551Glu 25225552:191:87
status: NEW