ABCMdb

PMID: 9346969

Ma J, Zhao J, Drumm ML, Xie J, Davis PB
Function of the R domain in the cystic fibrosis transmembrane conductance regulator chloride channel.
J Biol Chem. 1997 Oct 31;272(44):28133-41., [PubMed]

Sentences

No. Mutations Sentence Comment

258 ABCC7 p.Lys1250Ala ABCC7 p.Lys1250Met Point mutations within the conserved Walker A motif of NBF1 decreased the opening rate of the CFTR channel, while the corresponding mutations in NBF2 (K1250A, K1250M) prolong the open lifetime of CFTR (14, 15). Login to comment 259 ABCC7 p.Lys1250Ala ABCC7 p.Lys1250Ala ABCC7 p.Lys1250Met ABCC7 p.Lys1250Met The functional effects of K1250A and K1250M on the CFTR channel are similar to the effects of AMP-PNP and PPi (19, 24), suggesting that a decrease in the ATP hydrolysis rate at NBF2 leads to prolonged opening of the CFTR channel. Login to comment 260 ABCC7 p.Lys1250Ala ABCC7 p.Lys1250Met The functional effects of K1250A and K1250M on the CFTR channel are similar to the effects of AMP-PNP and PPi (19, 24), suggesting that a decrease in the ATP hydrolysis rate at NBF2 leads to prolonged opening of the CFTR channel. Login to comment