ABCMdb

PMID: 15366420

Zhang ZR, Zeltwanger S, McCarty NA
Steady-state interactions of glibenclamide with CFTR: evidence for multiple sites in the pore.
J Membr Biol. 2004 May 1;199(1):15-28., 2004-05-01 [PubMed]

Sentences

No. Mutations Sentence Comment

265 ABCC7 p.Lys1250Ala A recent study by Hwang and coworkers (Zhou et al., 2002) used the opposite approach in relying upon the K1250A-CFTR mutant that exhibits greatly diminished (but not completely abolished) ATP-dependent gating. Login to comment 309 ABCC7 p.Thr338Ala The most significant change was seen with the T338A mutant in transmembrane domain 6, although this only reflected a two-fold decrease in affinity. Login to comment 313 ABCC7 p.Lys1250Ala In that study, the behavior of mutant K1250A-CFTR was assayed with significant filtering of the single-channel records (100 Hz), resulting in loss of brief events. Login to comment 314 ABCC7 p.Lys1250Ala It is unclear whether this mutation, outside of the pore domain, might have any effect on block of the pore by glibenclamide; certainly, if glibenclamide binding is state-dependent, one would expect the results in K1250A-CFTR to differ substantially from those in wt-CFTR. Login to comment