ABCMdb

ABCC7 p.Cys343Ser

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Publications

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: 17036051 [PubMed] Mense M et al: "In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer."

No. Sentence Comment

180 CFTR with substitutions C128S, C225S, C343S and C866S was provided by Dr DC Dawson (OHSU, Portland, OR, USA). 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: 21796426 [PubMed] Holstead RG et al: "Functional Differences in Pore Properties Between Wild-Type and Cysteine-Less Forms of the CFTR Chloride Channel."

No. Sentence Comment

3 Our results suggest that the conductance difference is the result of a single substitution, of C343: the point mutant C343S has a conductance similar to cys-less, whereas the reverse mutation, S343C in a cys-less background, restores wild-type conductance levels. Login to comment
56 Single-channel conductance was also significantly increased in the point mutant C343S (P \ 0.0001) (Fig. 2), albeit to a slightly lesser degree than in cys-less (14.5 ± 2.7%, n = 8). Login to comment
57 In fact, the conductances of cys-less and C343S were not significantly different (P [ 0.4). Login to comment
67 As shown in Fig. 3, single-channel conductance was significantly reduced in C343L, significantly increased in C343A as well as C343S and not significantly changed in C343T and C343V. Login to comment
82 b, c Mean single channel I-V relationships recorded under these conditions for wild-type (filled circle, b), cys-less (open circle, b), C343S (filled circle, c) and cys-less S343C (open circle, c). Login to comment
122 Thus, the point mutation C343S causes an increase in conductance to a near cys-less level, whereas the revertant mutation S343C in a cys-less background reduces conductance to a near wild-type level (Fig. 2). Login to comment
138 Since C343T (unlike C343S) was not associated with a significant change in single-channel conductance (Fig. 3), a cys-less construct in which C343 is replaced by threonine, rather than serine, might be considered to retain wild-type channel properties more faithfully. Login to comment
139 However, since most other permeation properties of cys-less were found to be indistinguishable between wild-type and cys-less (containing the C343S mutation), it seems likely that in most respects it is functionally inconsequential if this site is a cysteine, serine or threonine. 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