ABCMdb

ABCC7 p.Cys524Ser

None has been submitted yet.

Publications

PMID: 16442101 [PubMed] Frelet A et al: "Insight in eukaryotic ABC transporter function by mutation analysis."

No. Sentence Comment

308 C524S has no effect. Login to comment

PMID: 15272010 [PubMed] Chen EY et al: "The DeltaF508 mutation disrupts packing of the transmembrane segments of the cystic fibrosis transmembrane conductance regulator."

No. Sentence Comment

57 The construction of Cys-less CFTR (C76S/C126S/C225S/C276S/C343S/C491S/C524S/C590S/C592S/C657S/C832S/C866S/C1344S/C1355S/C1395S/C1400S/C1410S/C1458S) was performed using the following cDNA fragments. Login to comment
58 Point mutations C76/126S were generated in sequence in the PstI (bp 1) 3 XbaI (bp 573) fragment; point mutations C225S/C276S/C343S were generated in sequence in the XbaI (bp 573) 3 KpnI (bp 1370) fragment; point mutations C491S/C524S/C590S/C592S/C657S were generated in sequence in the KpnI (bp 1370) 3 ApaI (bp 2333) fragment; point mutations C832S/C866S were generated in sequence in the ApaI (bp 2333) 3 EcoRI (bp 3643) fragment; point mutations C1344S/C1355S/ C1395S/C1400S/C1410S/C1458S were generated in sequence in the EcoRI (bp 3643) 3 XhoI (bp 4560) fragment, the five insert fragments were then ligated and inserted into the PstI and XhoI sites of plasmid vector pMT21. Login to comment

PMID: 19754156 [PubMed] Alexander C et al: "Cystic fibrosis transmembrane conductance regulator: using differential reactivity toward channel-permeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore."

No. Sentence Comment

42 The Cys-less CFTR construct (C76S, C126S, C225S, C276S, C343S, C491S, C524S, C590L, C592L, C657S, C832S, C866S, C1344S, C1355S, C1395S, C1400S, C1410S, C1458S) was a gift from Drs. Martin Mense and David Gadsby and was used in their pGEMHE vector previously described (13). Login to comment

PMID: 11867445 [PubMed] Harrington MA et al: "Cysteine residues in the nucleotide binding domains regulate the conductance state of CFTR channels."

No. Sentence Comment

72 C491S, C524S, C1344/1355S, and C491/524S mutants were inserted into a pcDNA3.1 expression vector and transiently transfected into HEK 293 cells using calcium phosphate. Login to comment
105 Mutation of C524 has little effect on channel gating While CFTR channels carrying the C491S mutation either alone or in combination with C524S or C1344/1355S open almost exclusively to a 3 pS subconductance, channels carry- ing only the C524S mutation exhibit conductance similar to wild-type channels. Login to comment
106 Like the wild-type channel, nearly every patch of C524S channels gates to the full-size openings, although, like wild-type channels, subconductance openings do appear (Table 1). Login to comment
107 Moreover, gating of the C524S mutant is sensitive to redox potential in a manner almost identical to that reported in wild-type channels, with the channel openings shortened by reducing conditions and oxidizing conditions resulting in long "locked open" bursts of the channel (Harrington et al., 1999). Login to comment
138 The patch was held at 75 mV. (B) Graph of open probability versus time for the patch shown in A. TABLE 1 Mutations of cysteine residues in NBD1 increase the proportion of patches with subconductance openings, while mutations of cysteines in NBD2 decrease the proportion of patches with subconductance openings Mutation Patches with Subconductance Patches with Full Size Total Patches Percent with Subconductance Percent with Full Size Wild-type 34 49 49 69 100 C491S 16 5 18 89 28 C491/524S 10 1 13 77 8 C524S 2 5 6 33 83 C1344/1355S 8 30 30 27 100 C-QUAD-S 19 0 30 63 0 The number of inside-out patches containing frequent full-size and/or subconductance channel openings were counted. Login to comment
204 Mutation of C491 in NBD1 to serine resulted in channels that opened almost exclusively to a 3-pS subconductance, while C524S mutant channels showed mostly full-size openings. Login to comment
206 The 3-pS subconductance of channels containing the C491S mutant alone or with other cysteine mutations was similar to the subconductance observed in recordings from patches containing wild-type CFTR channels, although with a shortened open dwell time. Login to comment
73 C491S, C524S, C1344/1355S, and C491/524S mutants were inserted into a pcDNA3.1 expression vector and transiently transfected into HEK 293 cells using calcium phosphate. Login to comment
108 Moreover, gating of the C524S mutant is sensitive to redox potential in a manner almost identical to that reported in wild-type channels, with the channel openings shortened by reducing conditions and oxidizing conditions resulting in long "locked open" bursts of the channel (Harrington et al., 1999). Login to comment
140 TABLE 1 Mutations of cysteine residues in NBD1 increase the proportion of patches with subconductance openings, while mutations of cysteines in NBD2 decrease the proportion of patches with subconductance openings Mutation Patches with Subconductance Patches with Full Size Total Patches Percent with Subconductance Percent with Full Size Wild-type 34 49 49 69 100 C491S 16 5 18 89 28 C491/524S 10 1 13 77 8 C524S 2 5 6 33 83 C1344/1355S 8 30 30 27 100 C-QUAD-S 19 0 30 63 0 The number of inside-out patches containing frequent full-size and/or subconductance channel openings were counted. Login to comment

PMID: 16766608 [PubMed] Serrano JR et al: "CFTR: Ligand exchange between a permeant anion ([Au(CN)2]-) and an engineered cysteine (T338C) blocks the pore."

No. Sentence Comment

23 MATERIALS AND METHODS Mutagenesis and in vitro transcription The Cys-less CFTR construct (C76S, C126S, C225S, C276S, C343S, C491S, C524S, C590L, C592L, C657S, C832S, C866S, C1344S, C1355S, C1395S, C1400S, C1410S, C1458S) was a gift from Drs. Martin Mense and Submitted December 28, 2005, and accepted for publication May 19, 2006. Login to comment

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

288 Of note, we were not able to express or purify NBD1 using the previously published mutations C491S, C524S, C590V, and C592V (12), probably because these mutations destabilize NBD1. Login to comment