ABCC7 p.Lys95His
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 25673337
[PubMed]
Rubaiy HN et al: "Location of a permeant anion binding site in the cystic fibrosis transmembrane conductance regulator chloride channel pore."
No.
Sentence
Comment
73
a Example macroscopic I-V relationships for K95H/E1371Q CFTR channels recorded using bath solutions at pH 5.5 (left) or pH 9.0 (right, different patch).
X
ABCC7 p.Lys95His 25673337:73:44
status: NEW75 b Mean KD values for Au(CN)2 - block of K95H/E1371Q at these two different pHs, obtained as described for Au(CN)2 - in Fig. 1.
X
ABCC7 p.Lys95His 25673337:75:40
status: NEW77 c Relationship between the observed KD values for Au(CN)2 - block (at -100 mV) and bath solution pH in K95H/ E1371Q and E1371Q.
X
ABCC7 p.Lys95His 25673337:77:103
status: NEW80 K95H0 refers to the unprotonated form of the histidine side chain (as expected at pH 9.0) and K95H?
X
ABCC7 p.Lys95His 25673337:80:94
status: NEW86 As shown in Fig. 3a and b, block of K95H/E1371Q by intracellular Au(CN)2 - was drastically stronger at pH 5.5 compared to pH 9.0, with the mean KD at -100 mV being increased 244-fold at the more alkaline pH.
X
ABCC7 p.Lys95His 25673337:86:36
status: NEW112 Removal of a positive charge in the pore inner vestibule by mutagenesis (in the K95Q mutant) or by increasing pH (in K95H) dramatically increases the apparent KD (Figs. 1, 2, 3, 4), suggesting that this positive charge is required for tight binding of permeant anions.
X
ABCC7 p.Lys95His 25673337:112:117
status: NEW113 In fact, since Au(CN)2 - , SCN- and C(CN)3 - are permeant anions and presumably have access to the entire pore, it is possible that the residual block observed in K95Q and in K95H (at pH 9.0) reflects interactions with a different part of the pore.
X
ABCC7 p.Lys95His 25673337:113:175
status: NEW