ABCC7 p.Tyr577His
| ClinVar: |
c.1731C>T
,
p.Tyr577=
D
, Likely pathogenic
c.1730A>T , p.Tyr577Phe ? , not provided |
| CF databases: |
c.1730A>T
,
p.Tyr577Phe
(CFTR1)
?
, Mutation Y577F and 1874insT were found together in another CF patient from Austria; this boy is also heterozygous for [delta]F508.
|
| Predicted by SNAP2: | A: D (59%), C: N (61%), D: D (71%), E: D (63%), F: N (82%), G: D (71%), H: N (78%), I: N (61%), K: D (63%), L: N (66%), M: N (53%), N: D (59%), P: D (80%), Q: N (57%), R: D (59%), S: D (63%), T: D (53%), V: N (66%), W: N (57%), |
| Predicted by PROVEAN: | A: N, C: N, D: N, E: N, F: N, G: N, H: N, I: N, K: N, L: N, M: N, N: N, P: N, Q: N, R: N, S: N, T: N, V: N, W: N, |
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[hide] Nucleotide-binding domains of human cystic fibrosi... Cell Mol Life Sci. 2004 Jan;61(2):230-42. Callebaut I, Eudes R, Mornon JP, Lehn P
Nucleotide-binding domains of human cystic fibrosis transmembrane conductance regulator: detailed sequence analysis and three-dimensional modeling of the heterodimer.
Cell Mol Life Sci. 2004 Jan;61(2):230-42., [PMID:14745501]
Abstract [show]
The cystic fibrosis transmembrane conductance regulator (CFTR) protein is encoded by the gene that is defective in cystic fibrosis, the most common lethal inherited disease among the Caucasian population. CFTR belongs to the ABC transporter superfamily, whose members form macromolecular architectures composed of two membrane-spanning domains and two nucleotide-binding domains (NBDs). The experimental structures of NBDs from several ABC transporters have recently been solved, opening new avenues for understanding the structure/function relationships and the consequences of some disease-causing mutations of CFTR. Based on a detailed sequence/structure analysis, we propose here a three-dimensional model of the human CFTR NBD heterodimer. This model, which is in agreement with recent experimental data, highlights the specific features of the CFTR asymmetric active sites located at the interface between the two NBDs. Moreover, additional CFTR-specific features can be identified at the subunit interface, which may play critical roles in active site interdependence and are uncommon in other NBD dimers.
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No. Sentence Comment
221 This model of interaction is further supported by phylogenetic analysis of CFTR sequences [49], in which substitution of His1348 by Asn in fish sequences (dogfish, salmon, and killifish) appears to be correlated to substitution of Tyr577 by His.
X
ABCC7 p.Tyr577His 14745501:221:231
status: NEW