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
X
ABCC7 p.Lys1250Ala 15366420:265:105
status: NEW
view ABCC7 p.Lys1250Ala details
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
X
ABCC7 p.Thr338Ala 15366420:309:46
status: NEW
view ABCC7 p.Thr338Ala details
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
X
ABCC7 p.Lys1250Ala 15366420:313:38
status: NEW
view ABCC7 p.Lys1250Ala details
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
X
ABCC7 p.Lys1250Ala 15366420:314:214
status: NEW
view ABCC7 p.Lys1250Ala details
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