ABCMdb

ABCC7 p.His1350Ala

None has been submitted yet.

Publications

PMID: 9558482 [PubMed] Foskett JK et al: "ClC and CFTR chloride channel gating."

No. Sentence Comment

323 Mutation of this residue to glutamine (H1350Q; predicted to increase ATP hydrolysis rate) but not to alanine (H1350A; predicted to have no effect on hydrolysis) destabilized the open state (138), again supporting a role for hydrolysis at NBD2 in controlling the duration of the open state. Login to comment

PMID: 8599650 [PubMed] Carson MR et al: "Structural and functional similarities between the nucleotide-binding domains of CFTR and GTP-binding proteins."

No. Sentence Comment

27 To test these hypotheses we used the excised inside-out patch-clamp technique to study CFTR variants containing the Q552A, Q552H, H1350Q, and H1350A mutations. Login to comment
77 Open circles, wild-type; open triangles, Q552A; open squares, Q552H; filled circles, H1350A; filled triangles, H1350Q. Login to comment
90 Fig. 2 A shows 0.250- B. 2000- mean closed-time between 1000- bursts (ms) 0- C. mean burst duration (ms) wild-type T T k" IffilI -.. wild- Q552A 0552H H1350Q H1350A type 3001 wilt'- type FIGURE 3 Effect of mutation of Q552 and H1350 on single channel activity. Login to comment
113 Fig. 4 shows that ADP inhibited ATP-supported current in the A. H1350A NBD2 mutants to an extent similar to that observed with wild-type CFTR. Login to comment
124 A, Time course of macroscopic current in excised membrane patches from cells expressing either H1350A (top panel) or H1350Q (bottom panel) channels. Login to comment
129 There was no difference between groups (p > 0.3 for all, n = 4, 3, and 3 for wild-type, H1350A, and H1350Q, respectively). Login to comment
131 'Wo I (pA) 150 0 1.5 3.0 4.5 6.0 7.5 time (min) 75- 50- % Inhibition by ADP 250- wild- H1350A H1350Q type Carson and Welsh Similarity between CFTR and GTP-Binding Proteins 2447 from the nucleotide-binding site. Login to comment