ABCMdb

PMID: 9454574

Wigley WC, Vijayakumar S, Jones JD, Slaughter C, Thomas PJ
Transmembrane domain of cystic fibrosis transmembrane conductance regulator: design, characterization, and secondary structure of synthetic peptides m1-m6.
Biochemistry. 1998 Jan 20;37(3):844-53., [PubMed]

Sentences

No. Mutations Sentence Comment

261 ABCC7 p.Pro574His ABCC7 p.Ala455Glu ABCC7 p.Pro205Ser The critical importance of this intramembrane residue to CFTR structure is highlighted by the CF-causing mutation of proline 205 to serine (54), which prevents proper folding and processing of CFTR (52) and causes a form of cystic fibrosis similar to other misprocessing mutants such as A455E and P574H (55). Login to comment 287 ABCC7 p.Arg347His ABCC7 p.Lys335Glu For example, mutational data demonstrated that the substitution of glutamic acid for lysine 335 alters channel permeability of CFTR (4), and mutation of arginine 347 to histidine gives rise to pH-dependent ion selectivity of the channel (66). Login to comment