ABCMdb

PMID: 9711592

King SA, Sorscher EJ
Recombinant synthesis of cystic fibrosis transmembrane conductance regulator and functional nucleotide-binding domains.
Methods Enzymol. 1998;292:686-97., [PubMed]

Sentences

No. Mutations Sentence Comment

53 ABCC7 p.Gly551Asp Many of the mutant proteins, including a glycine ~ aspartic acid replacement at CFTR postion 551 (G551D), have suppressed chloride conductance.3-5 Although AF508 CFTR may have nearly normal anion conductance properties, disease associated with this allele is believed to result from a failure to process the AF508 protein beyond the ER to the Golgi apparatus; instead the protein is degraded very rapidly through a mechanism that appears to involve the ubiquitin/proteasome pathway.3,4 Intrinsic properties of wild-type and mutant NBD1 and related CFTR peptides have been studied in an attempt to understand the effects of regional mutations on CFTR function and biogenesis. Login to comment 191 ABCC7 p.Lys464Met For example, a glycine ~ aspartic acid replacement at CFTR position 551 within a highly conserved ABC protein motif (LSGGQXQR, glycine corresponding to position 551 underlined) disrupts the nucleotide interaction.5 The same appears to be true when a critical lysine residue in the Walker A site of NBD1 is substituted for methionine (K464M.) Login to comment 198 ABCC7 p.Gly551Asp ABCC7 p.Lys464Met Maximal binding for the wild-type NBD1 was approximately four times that of the G551D and K464M domains. Login to comment