ABCMdb

PMID: 25120007

Tripathi R, Benz N, Culleton B, Trouve P, Ferec C
Biophysical characterisation of calumenin as a charged F508del-CFTR folding modulator.
PLoS One. 2014 Aug 13;9(8):e104970. doi: 10.1371/journal.pone.0104970. eCollection 2014., [PubMed]

Sentences

No. Mutations Sentence Comment

33 ABCC7 p.Gly551Asp ABCC7 p.Gly551Asp Recently, calumenin, belonging to the CREC (abbreviation for Cab45, reticulocalbin, ERC-45 and calumenin) family of low affinity calcium binding proteins containing multiple EF-hands, has been identified as a putative G551D-CFTR (Gly to Asp mutation at position 551) chaperone [12]. Login to comment 35 ABCC7 p.Gly551Asp Besides associating specifically with G551D-CFTR, calumenin is also predicted to interact with wild-type CFTR [12]. Login to comment 42 ABCC7 p.Gly551Asp ), calcium binding proteins (such as calgranulin, PSOR1, PDCD6), wild-type and mutant CFTR sequences (F508del-CFTR, G551D-CFTR) and five previously described intrinsically disordered proteins (IDPs) [15-17]. Login to comment 105 ABCC7 p.Gly551Asp CFTR variants (wild type, F508del, G551D) and intrinsically disordered proteins (IDPs) were also used in this analysis due to their extremely high and low hydropathy values respectively. Login to comment 307 ABCC7 p.Ile539Thr ABCC7 p.Gly550Glu Further insights into the design parameters for such peptides are gained by the observation that certain suppressor mutations such as G550E and I539T can partially rescue the F508del-CFTR to the cell surface [6]. Login to comment