ABCMdb

ABCC7 p.Arg1358Ala

None has been submitted yet.

Publications

PMID: 20876359 [PubMed] Szollosi A et al: "Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2."

No. Sentence Comment

18 We expressed wild-type as well as F1296S, N1303Q, and R1358A mutant CFTR in Xenopus oocytes and studied these channels using macroscopic inside-out patch recordings. Login to comment
112 Fig. S7 shows example macroscopic current traces to illustrate the apparent affinities of R1358A and R1358A/N1303Q for ATP. Login to comment
129 To perturb site 3, we chose mutation R1358A, which is likely to prevent a possible hydrogen-bonding interaction between the R1358 and N1303 side chains. Login to comment
186 (A) Representative traces of R1358A and R1358A/N1303Q currents illustrating segments in 0 mM ATP and bracketing segments in 2 mM ATP. Dotted lines show zero current level. Login to comment
187 (B) Estimation of Po;max for WT (black), R1358A (red), N1303Q (blue), and R1358A/N1303Q (green) by stationary noise analysis. Login to comment
188 Estimated Po;max was 0.62 ± 0.05 for R1358A and 0.36 ± 0.04 for R1358A/N1303Q. Login to comment
191 (E) ATP-dependent current fractions (II0)/(ImaxI0) plotted as a function of [ATP] for WT (black), R1358A (red), N1303Q (blue), and R1358A/N1303Q (green). Login to comment
196 Combining Po;bas/Po;max, obtained from current segments in 0 mM and bracketing periods in 2 mM ATP with Po;max estimated for the 2-mM ATP segments using stationary noise analysis (Fig. 7 B), provided Po;bas estimates (Fig. 7 C) that were higher in both R1358A and R1358A/N1303Q compared with WT or N1303Q. Login to comment
199 We also investigated a possible change in coupling between sites 2 and 3 upon ATP binding by studying [ATP] dependence of macroscopic currents (sample current traces for R1358A and R1358A/N1303Q are shown in Fig. S7, A and B). Login to comment
200 Fitting the [ATP] dose-response curve of the ATP-sensitive current fractions (Fig. 7 E) yielded a slightly increased KPo value for R1358A/N1303Q (inset), but for the calculated KrCO values (Fig. 7 F), a similar trend was apparent even for R1358A. Login to comment
214 Truncation of the site-3 arginine side chain promotes spontaneous, ATP-independent opening regardless of the side chain at site 2 To determine the functional importance of site 3 within our triad of target residues (Fig. 1), we investigated functional coupling between sites 2 (position 1303) and 3 (position 1358) by comparing the effects of removal of the R1358 side chain (R1358A) in either a WT or an N1303Q background. Login to comment
215 Interestingly, after prephosphorylation by 300 nM PKA, both R1358A and R1358A/N1303Q result from formation of a stabilizing interaction in state B (or breaking of a destabilizing interaction present in state A). Login to comment
281 The observed facilitation of spontaneous channel openings by the R1358A mutation (Fig. 7 C) therefore likely reflects loss of a stabilizing interaction in the C1 state between R1358 and a residue other than N1303. Login to comment

PMID: 24058550 [PubMed] Dawson JE et al: "Allosteric coupling between the intracellular coupling helix 4 and regulatory sites of the first nucleotide-binding domain of CFTR."

No. Sentence Comment

265 ATP-independent channel opening has been enhanced by Cys, Ser, and Pro mutations of K978 in the ICDs [15] and F1296S/N1303Q and R1358A in NBD2 [60]. Login to comment