ABCC7 p.Ser712Cys
| CF databases: |
c.2135C>G
,
p.Ser712Cys
(CFTR1)
?
,
|
| Predicted by SNAP2: | A: N (72%), C: D (53%), D: D (71%), E: D (66%), F: D (71%), G: N (72%), H: D (63%), I: N (53%), K: D (71%), L: D (71%), M: D (63%), N: N (53%), P: D (71%), Q: D (59%), R: D (71%), T: N (78%), V: D (66%), W: D (80%), Y: D (71%), |
| Predicted by PROVEAN: | A: N, C: D, D: N, E: N, F: D, G: N, H: N, I: D, K: N, L: D, M: N, N: N, P: D, Q: N, R: N, T: N, V: D, W: D, Y: D, |
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[hide] CFTR regulatory region interacts with NBD1 predomi... Nat Struct Mol Biol. 2007 Aug;14(8):738-45. Epub 2007 Jul 29. Baker JM, Hudson RP, Kanelis V, Choy WY, Thibodeau PH, Thomas PJ, Forman-Kay JD
CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices.
Nat Struct Mol Biol. 2007 Aug;14(8):738-45. Epub 2007 Jul 29., [PMID:17660831]
Abstract [show]
The regulatory (R) region of the cystic fibrosis transmembrane conductance regulator (CFTR) is intrinsically disordered and must be phosphorylated at multiple sites for full CFTR channel activity, with no one specific phosphorylation site required. In addition, nucleotide binding and hydrolysis at the nucleotide-binding domains (NBDs) of CFTR are required for channel gating. We report NMR studies in the absence and presence of NBD1 that provide structural details for the isolated R region and its interaction with NBD1 at residue-level resolution. Several sites in the R region with measured fractional helical propensity mediate interactions with NBD1. Phosphorylation reduces the helicity of many R-region sites and reduces their NBD1 interactions. This evidence for a dynamic complex with NBD1 that transiently engages different sites of the R region suggests a structural explanation for the dependence of CFTR activity on multiple PKA phosphorylation sites.
Comments [show]
None has been submitted yet.
No. Sentence Comment
149 Milder phenotypes are seen for many cystic fibrosis-causing CFTR missense mutations within the R region, consistent with this multisite behavior, and the majority of these mutations are at the PKA recognition and phosphorylation sites (R709N, S712C, R735K, S737F, V754M, R766M, R810G and S813P; http://www.
X
ABCC7 p.Ser712Cys 17660831:149:243
status: NEW