ABCC7 p.Ala96Val
| ClinVar: |
c.287C>A
,
p.Ala96Glu
?
, not provided
|
| CF databases: |
c.287C>A
,
p.Ala96Glu
(CFTR1)
?
, This mutation was found in a Turkish patient.
|
| Predicted by SNAP2: | C: N (61%), D: D (80%), E: D (80%), F: D (80%), G: D (66%), H: D (85%), I: N (53%), K: D (85%), L: D (53%), M: D (53%), N: D (71%), P: D (66%), Q: D (75%), R: D (80%), S: N (78%), T: N (78%), V: N (78%), W: D (85%), Y: D (80%), |
| Predicted by PROVEAN: | C: N, D: N, E: N, F: N, G: N, H: N, I: N, K: N, L: N, M: N, N: N, P: N, Q: N, R: N, S: N, T: N, V: N, W: N, Y: N, |
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[hide] Direct comparison of the functional roles played b... J Biol Chem. 2004 Dec 31;279(53):55283-9. Epub 2004 Oct 25. Ge N, Muise CN, Gong X, Linsdell P
Direct comparison of the functional roles played by different transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore.
J Biol Chem. 2004 Dec 31;279(53):55283-9. Epub 2004 Oct 25., 2004-12-31 [PMID:15504721]
Abstract [show]
The cystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channel contains 12 transmembrane (TM) regions that are presumed to form the channel pore. However, little is known about the relative functional contribution of different TM regions to the pore. We have used patch clamp recording to investigate the functional consequences of point mutations throughout the six transmembrane regions in the N-terminal part of the CFTR protein (TM1-TM6). A range of specific functional assays compared the single channel conductance, anion binding, and anion selectivity properties of different channel variants. Overall, our results suggest that TM1 and -6 play dominant roles in forming the channel pore and determining its functional properties, with TM5 perhaps playing a lesser role. In contrast, TM2, -3, and -4 appear to play only minor supporting roles. These results define transmembrane regions 1 and 6 as major contributors to the CFTR channel pore and have strong implications for emerging structural models of CFTR and related ATP-binding cassette proteins.
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No. Sentence Comment
44 Preliminary studies showed that some such mutations in TM1 did not yield expression of functional channels, and in these cases more conservative substitutions were employed (i.e. T94S, K95Q, A96V).
X
ABCC7 p.Ala96Val 15504721:44:191
status: NEW109 Thiocyanate permeability was strongly increased in A96V and T338A, suggesting enhancement of lyotropic selectivity in these mutants, and dramatically reduced in F337A, which we previously suggested reflects the role of Phe-337 in contributing to an anion selectivity filter in the pore (11, 36).
X
ABCC7 p.Ala96Val 15504721:109:51
status: NEW154 However, the amplitude-independent current reversal potentials reflect an increased SCN- relative permeability (PSCN/PCl) in A96V and a diminished PSCN/PCl in F337A compared with wild type.
X
ABCC7 p.Ala96Val 15504721:154:125
status: NEW