ABCC7 p.Asp572Met
| ClinVar: |
c.1714G>A
,
p.Asp572Asn
?
, not provided
|
| CF databases: |
c.1714G>A
,
p.Asp572Asn
(CFTR1)
?
, The nucleotide change G->A at nucleotide position 1846 leads to D572N in exon 12. This variation was observed on one CF chromosome in collaboration with Dr Kapranov (Moscow, Russia)
c.1714G>C , p.Asp572His (CFTR1) ? , |
| Predicted by SNAP2: | A: D (95%), C: D (95%), E: D (95%), F: D (95%), G: D (95%), H: D (95%), I: D (95%), K: D (95%), L: D (95%), M: D (95%), N: D (53%), P: D (95%), Q: D (95%), R: D (95%), S: D (95%), T: D (95%), V: D (95%), W: D (95%), Y: D (95%), |
| Predicted by PROVEAN: | A: D, C: D, E: D, F: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, Q: D, R: D, S: D, T: D, V: D, W: D, Y: D, |
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[hide] Nucleotide-binding domain 1 of cystic fibrosis tra... Eur J Biochem. 2000 Sep;267(17):5306-12. Duffieux F, Annereau JP, Boucher J, Miclet E, Pamlard O, Schneider M, Stoven V, Lallemand JY
Nucleotide-binding domain 1 of cystic fibrosis transmembrane conductance regulator production of a suitable protein for structural studies.
Eur J Biochem. 2000 Sep;267(17):5306-12., [PMID:10951189]
Abstract [show]
Cystic fibrosis is caused by mutations in the gene encoding the cystic fibrosis transmembrane conductance regulator (CFTR). This protein belongs to the large ATP-binding cassette (ABC) family of transporters. Most patients with cystic fibrosis bear a mutation in the nucleotide-binding domain 1 (NBD1) of CFTR, which plays a key role in the activation of the channel function of CFTR. Determination of the three dimensional structure of NBD1 is essential to better understand its structure-function relationship, and relate it to the biological features of CFTR. In this paper, we report the first preparation of recombinant His-tagged NBD1, as a soluble, stable and isolated domain. The method avoids the use of renaturing processes or fusion constructs. ATPase activity assays show that the recombinant domain is functional. Using tryptophan intrinsic fluorescence, we point out that the local conformation, in the region of the most frequent mutation DeltaF508, could differ from that of the nucleotide-binding subunit of histidine permease, the only available ABC structure. We have undertaken three dimensional structure determination of NBD1, and the first two dimensional 15N-1H NMR spectra demonstrate that the domain is folded. The method should be applicable to the structural studies of NBD2 or of other NBDs from different ABC proteins of major biological interest, such as multidrug resistance protein 1 or multidrug resistance associated protein 1.
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No. Sentence Comment
40 Synthetic mutated oligonucleotides (Eurogentec) were K464M: 5H -CCACTGGAGCAGGCATGA- CTTCACTTCTAATGGTG-3H and D572M: 5H -GCTGATTTGT- ATTTATTAATGTCTCCTTTTGGATACC-3H , where underlined nucleotides represent mutations.
X
ABCC7 p.Asp572Met 10951189:40:109
status: NEW116 Mutations were introduced in the Walker A and B motifs (K464M, D572M), at positions known to be involved in ATP binding and hydrolysis [21].
X
ABCC7 p.Asp572Met 10951189:116:63
status: NEW