ABCMdb

ABCC7 p.Pro205Leu

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
42 Consistent with this conclusion, full-length P205L mutant CFTR expressed in cultured cells also misfolds, fails to achieve mature glycosylation and is retained in the ER (W.C.W., M.J.C. and P.J.T., unpublished observations). 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
72 Constructs are denoted as follows: P, TfR-m3 wt; S, TfR-m3 P205S; and L, TfR-m3 P205L. Login to comment
92 Consistent with the peptide results, the wild type chimera properly integrates better than either the P205S or P205L mutants (Fig. 3b). Login to comment
133 A representative IR spectrum (solid line) of the amide I region is presented for the mutant peptide (P205L). Login to comment
136 b, Wild type and mutant (P205L) peptides were first solubilized in neat TFE at 5 mg ml-1 and then unfolded by rapid dilution (1/10) in the strong denaturant 6 M guanidinium-SCN. Login to comment
142 The symbols used are wild type (filled circle) and P205L (open circle). Login to comment