ABCC7 p.Leu15Pro
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PMID: 20100616
[PubMed]
Havasi V et al: "Association of cystic fibrosis genetic modifiers with congenital bilateral absence of the vas deferens."
No.
Sentence
Comment
68
Portuguese CFTR alleles Spanish CFTR alleles Turkish CFTR alleles 5T 22 F508del 11 5T 20 F508del 14 5T 9 D1152H 14 R334W 5 D443Ya 3 D110H 3 R117H 3 G576Aa 3 F508del 2 S1235R 3 R668Ca 3 3041-11del7 2 N1303K 2 G542X 2 1767del6 2 P205S 2 R117H 2 2789þ5G>A 2 D614G 2 V232D 2 CFTRdele2(ins186) 2 G542X 1 L997F 1 3120þ1G>A 1 L206W 1 H609R 1 G1130A 1 V562I 1 N1303H 1 M952I 1 I507del 1 L206W 1 365insT 1 3272-26A>G 1 3272-26A/G 1 E585X 1 2789þ5G>A 1 L15P 1 2752-15C>G 1 G576Aa 1 R347H 1 R334Q 1 R668Ca 1 2689insG 1 R347H 1 CFTRdele2,3 1 R1070W 1 E831X 1 L1227S 1 I 1027T 1 R1070W 1 E831X 1 3272-26A>G 1 L997F 1 I853F 1 A349V 1 6T 1 Note: CFTR ¼ cystic fibrosis transmembrane conductance regulator.
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ABCC7 p.Leu15Pro 20100616:68:458
status: NEW
PMID: 20351098
[PubMed]
Playford MP et al: "Cystic fibrosis transmembrane conductance regulator interacts with multiple immunoglobulin domains of filamin A."
No.
Sentence
Comment
5
Point and deletion mutants of IgFLNa and CFTR informed by the models, including disease-causing mutations L15P and W19C, disrupted the binding interaction.
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ABCC7 p.Leu15Pro 20351098:5:106
status: NEW113 Amino acid changes reflecting known CF mutations within this peptide (S13F, L15P, or W19C) prevented FLNa binding (Fig. 5C).
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ABCC7 p.Leu15Pro 20351098:113:76
status: NEW125 Red and blue amino acids indicate residues mutated in CF patients (P5L, S13F, L15P, and W19C).
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ABCC7 p.Leu15Pro 20351098:125:78
status: NEW137 The model also predicted that CF-causing L15P and W19C but not P5L mutants of CFTR perturb the interaction with FLNa.
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ABCC7 p.Leu15Pro 20351098:137:41
status: NEW138 Indeed, L15P and W19C synthetic CFTR1-20 peptides did not or barely bound FLNa (Fig. 5C).
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ABCC7 p.Leu15Pro 20351098:138:8
status: NEW142 The wild-type, L15P, and W19C peptides were soluble at least at concentration of 1 mg/ml in PBS.
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ABCC7 p.Leu15Pro 20351098:142:15
status: NEW153 C, effect of CF-causing point mutations of CFTR on FLNa binding.OnemlofPBSwasaddedto1mgofbiotinylatedCFTR1-20peptides(wild-type,P5L,L15P,andW19C), andthesolutionwascentrifugedat15,000ϫgfor10minatroomtemperature.Allofthepeptidesweresoluble except for P5L mutant peptide (asterisk).
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ABCC7 p.Leu15Pro 20351098:153:132
status: NEW227 Structural Basis for Mutations That Impair the FLNa-CFTR Interaction-Three missense mutations in the FLNa-binding site of CFTR have been reported: S13F, L15P, and W19C.
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ABCC7 p.Leu15Pro 20351098:227:153
status: NEW229 The model also predicts that CF-causing L15P and W19C mutations in CFTR perturb the interaction with FLNa.
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ABCC7 p.Leu15Pro 20351098:229:40
status: NEW230 Mutation of Leu-15 to Pro dramatically changes the structure of the CFTR peptide.
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ABCC7 p.Leu15Pro 20351098:230:12
status: NEW
No.
Sentence
Comment
872
Importantly, two CF disease-causing mutations, L15P and W19C, disrupt the interaction between filamin A and CFTR (Playford et al., 2010).
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ABCC7 p.Leu15Pro 24685681:872:47
status: NEW