ABCC7 p.Trp1310His
| ClinVar: |
c.3929G>A
,
p.Trp1310*
?
, not provided
|
| Predicted by SNAP2: | A: D (63%), C: N (72%), D: D (63%), E: D (53%), F: N (78%), G: D (63%), H: N (82%), I: N (57%), K: N (53%), L: N (66%), M: N (57%), N: N (57%), P: D (53%), Q: N (66%), R: N (57%), S: N (53%), T: N (53%), V: N (61%), Y: N (87%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: N, G: D, H: N, I: D, K: D, L: D, M: N, N: D, P: D, Q: N, R: D, S: D, T: D, V: D, Y: N, |
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[hide] Cystic fibrosis transmembrane conductance regulato... Cold Spring Harb Perspect Med. 2013 Feb 1;3(2):a009514. doi: 10.1101/cshperspect.a009514. Hunt JF, Wang C, Ford RC
Cystic fibrosis transmembrane conductance regulator (ABCC7) structure.
Cold Spring Harb Perspect Med. 2013 Feb 1;3(2):a009514. doi: 10.1101/cshperspect.a009514., [PMID:23378596]
Abstract [show]
Structural studies of the cystic fibrosis transmembrane conductance regulator (CFTR) are reviewed. Like many membrane proteins, full-length CFTR has proven to be difficult to express and purify, hence much of the structural data available is for the more tractable, independently expressed soluble domains. Therefore, this chapter covers structural data for individual CFTR domains in addition to the sparser data available for the full-length protein. To set the context for these studies, we will start by reviewing structural information on model proteins from the ATP-binding cassette (ABC) transporter superfamily, to which CFTR belongs.
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No. Sentence Comment
289 Improvements in the yield of soluble protein were obtained by introducing the hydrolytically inactivating H1402A mutation in ATPase active site of hNBD2 plus a series of "solubilizing" mutations on its surface (Q1280E/ Y1307N/W1310H/Q1411D) (X Zhao, S Atwell, JF Hunt, et al., unpubl.).
X
ABCC7 p.Trp1310His 23378596:289:226
status: NEW