ABCMdb

ABCC7 p.Pro205Ala

None has been submitted yet.

Publications

PMID: 11938353 [PubMed] Wigley WC et al: "A protein sequence that can encode native structure by disfavoring alternate conformations."

No. Sentence Comment

41 This alternate conformation is apparently not induced specifically by the Ser residue, because the control peptides (P205G, P205A and P205L) each assume a similar non-native structure under these conditions. Login to comment
49 CD spec- troscopy30 evaluated the seconday structure of peptides representing wild type m3, the CF-causing mutant P205S, and control peptides P205G, P205A and P205L solubilized in either micellar SDS (0.5% (w/v) SDS and 5mM phosphate buffer, pH 7.2) or polyfluorinated organic solvents (10% HFIP, 40% TFE and 50% (v/v) H2O). Login to comment
50 The lines used to represent each peptide are wild type m3, dashed red; P205S, dashed blue; P205G, solid green; P205A, solid light purple; and P205L, solid black. Login to comment
104 In each of four mutant peptides, Pro 205 was replaced by an Ala, and extant Ala residues at positions 196 (red), 198 (blue), 204 (green) or 209 (light purple) were individually replaced with Pro. Login to comment

PMID: 19181854 [PubMed] Rath A et al: "Detergent binding explains anomalous SDS-PAGE migration of membrane proteins."

No. Sentence Comment

45 Five mutants (A204L, P205A/ Table 1. Login to comment
61 PA/VD and ES/SE denote the P205A/V232D and E217S/S222E hairpins, respectively. Login to comment
97 PA/VD and ES/SE denote the P205A/V232D and E217S/S222E hairpins, respectively. Login to comment
123 However, even if SDS/ protein stoichiometry (and by extension, gel shift) remains unchanged, increases in the conformational flexibility of non-coated regions may alter the hairpin`s hydrodynamic radius (compare Fig. 5 B-E)-a potential explanation for the as-WT gel shift but increased hydrodynamic radius relative to WT of the P205A/V232D mutant. Login to comment
141 For example, V232D and P205A/V232D display larger than WT hydrodynamic radii on SEC-HPLC (ϩ19% and ϩ21%, respectively)-even though each Asp-containing mutant migrates faster or as-WT on PAGE. Login to comment

PMID: 8663008 [PubMed] Sheppard DN et al: "Contribution of proline residues in the membrane-spanning domains of cystic fibrosis transmembrane conductance regulator to chloride channel function."

No. Sentence Comment

122 Mutant n Px/PCl Gx/GCl Br- Cl- IBr- ClI- CFTR 5 1.18 Ϯ 0.08 1.00 0.73 Ϯ 0.05 1.27 Ϯ 0.16 1.00 0.61 Ϯ 0.08 P99A 7 0.98 Ϯ 0.03 1.00 0.70 Ϯ 0.06 1.04 Ϯ 0.05 1.00 0.72 Ϯ 0.05 P99G 5 1.06 Ϯ 0.02 1.00 0.75 Ϯ 0.08 1.04 Ϯ 0.07 1.00 0.66 Ϯ 0.05 P99L 5 1.21 Ϯ 0.07 1.00 1.06 Ϯ 0.07 1.33 Ϯ 0.11 1.00 0.95 Ϯ 0.08 P205A 4 1.09 Ϯ 0.07 1.00 0.64 Ϯ 0.09 0.95 Ϯ 0.04 1.00 0.46 Ϯ 0.11 P205G 5 1.09 Ϯ 0.05 1.00 0.45 Ϯ 0.05 1.05 Ϯ 0.03 1.00 0.44 Ϯ 0.06 P205S 2 1.01 Ϯ 0.01 1.00 0.55 Ϯ 0.28 1.09 Ϯ 0.09 1.00 0.59 Ϯ 0.08 P324A 7 1.08 Ϯ 0.04 1.00 0.72 Ϯ 0.06 1.15 Ϯ 0.07 1.00 0.60 Ϯ 0.08 P324G 6 1.12 Ϯ 0.07 1.00 0.69 Ϯ 0.04 1.22 Ϯ 0.14 1.00 0.57 Ϯ 0.04 P1021A 3 1.15 Ϯ 0.17 1.00 0.73 Ϯ 0.11 1.17 Ϯ 0.10 1.00 0.47 Ϯ 0.19 P1021G 7 1.17 Ϯ 0.06 1.00 0.78 Ϯ 0.02 1.21 Ϯ 0.08 1.00 0.59 Ϯ 0.06 though for P99G the reduction was small, for P99A and P99L the effect was marked. Login to comment
126 The conductance for P99G was 7.31 Ϯ 0.24 pS (n ϭ 5), not significantly different from wild type (p ϭ 0.26). Login to comment
145 The number of cells responding to cAMP agonists with Cl- current activation relative to the total number of cells tested for each construct was: CFTR (8/16; 50%), P99A (11/12; 92%), P99G (9/19; 47%), P99L (10/19; 53%), P205A (7/12; 58%), P205G (5/9; 56%), P205S (7/20; 35%), P324A (9/18; 50%), P324G (9/22; 41%), P1021A (8/18; 44%), and P1021G (7/16; 44%). Login to comment
149 The number of cells responding to cAMP agonists with Cl2 current activation relative to the total number of cells tested for each construct was: CFTR (8/16; 50%), P99A (11/12; 92%), P99G (9/19; 47%), P99L (10/19; 53%), P205A (7/12; 58%), P205G (5/9; 56%), P205S (7/20; 35%), P324A (9/18; 50%), P324G (9/22; 41%), P1021A (8/18; 44%), and P1021G (7/16; 44%). Login to comment