ABCC7 p.Phe409Leu

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PMID: 15528182 [PubMed] Lewis HA et al: "Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure."
No. Sentence Comment
100 Crystal Structure of ⌬F508 hNBD1 Shows Minimal Conformational Changes but Substantive Changes in Surface Topography at the Putative Site of MSD1 Interaction-Crystals diffracting to a resolution of 2.3 Å were obtained for hNBD1-7a- ⌬F508, which contains seven mutations (F409L, F429S, F433L, G550E, R553Q, R555K, H667R) in addition to the deletion of Phe-508 (see Table II).
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ABCC7 p.Phe409Leu 15528182:100:289
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138 Of the seven solubilizing mutations present in the ⌬F508 form of hNBD1, three (F409L, F429S, F433L) occur in disordered regions and therefore likely interact with solvent, whereas residue H667R is only minimally solvent-exposed on the surface of ␣-helix 9b in the RE.
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ABCC7 p.Phe409Leu 15528182:138:86
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PMID: 15619636 [PubMed] Thibodeau PH et al: "Side chain and backbone contributions of Phe508 to CFTR folding."
No. Sentence Comment
148 Note added in proof: Crystal structures of the human F508A missense NBD1 (with solublizing mutations F429S and H667R) and the corrected ∆F508 NBD1 (with three known suppressor mutations G550E, R553Q and R555K, and the solublizing mutations F409L, F429S, F433L and H667R) have been reported51.
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ABCC7 p.Phe409Leu 15619636:148:247
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PMID: 18597042 [PubMed] Mornon JP et al: "Atomic model of human cystic fibrosis transmembrane conductance regulator: membrane-spanning domains and coupling interfaces."
No. Sentence Comment
97 These mutations are actually located outside the NBD1 structure core, in the regulatory insertion (F409L, F429S, F433L) and extension (R667H), or in the signature sequence region (G550E, R553Q, R555K), whose local conformations in the crystal structure and in our model are perfectly superimposable.
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ABCC7 p.Phe409Leu 18597042:97:99
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PMID: 19781595 [PubMed] Bisignano P et al: "Molecular dynamics analysis of the wild type and dF508 mutant structures of the human CFTR-nucleotide binding domain 1."
No. Sentence Comment
20 Structures were obtained by X-ray crystallography, at a resolution of 2.55 Å and 2.30 Å for WT and mutant, respectively. These structures are both characterized by the presence of seven mutations: F409L, F429S, F433L, G550E, R553Q, R555K and H667R which make them more soluble and therefore more easily crystallizable [6,7].
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ABCC7 p.Phe409Leu 19781595:20:207
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152 The chosen PDB entries,1XMJ and 2BBO, contain seven mutations, F409L, F429S, F433L, G550E, R553Q, R555K and H667R, that were introduced to the NBD1, wild type and dF508 used for this study, to facilitate the crystallization of the polypeptide [6].
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ABCC7 p.Phe409Leu 19781595:152:63
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PMID: 19944699 [PubMed] Lewis HA et al: "Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry."
No. Sentence Comment
325 Not shown here are three residues that were mutated in various constructs but located in the disordered region of the RI (i.e., the F429S mutation present in constructs 2b, 3, and 7a and the F409L and F433L mutations present in construct 7a).
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ABCC7 p.Phe409Leu 19944699:325:191
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PMID: 20150177 [PubMed] Atwell S et al: "Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant."
No. Sentence Comment
226 The 389-678(F409L, F429S, F433L, G550E, R553Q, R555K, H667R) (hNBD1-7a) structures are shown without (dark blue) and with the DF508 mutation (light blue) (H. Lewis, in preparation).
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ABCC7 p.Phe409Leu 20150177:226:12
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249 Many of the solubilizing mutations developed for non-truncated NBD1 are in the RI or Q-loop cleft (F409L, F429S, F433L and F494N) and might function by reducing these interactions.
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ABCC7 p.Phe409Leu 20150177:249:99
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PMID: 22265408 [PubMed] Rabeh WM et al: "Correction of both NBD1 energetics and domain interface is required to restore DeltaF508 CFTR folding and function."
No. Sentence Comment
26 Both the R mutations (G550E, R553Q, and R555K) and S mutations (F409L, F429S, F433L, F494N, and H667R) could partially rescue the DF508 CFTR folding and functional defect (Lewis et al., 2005; Pissarra et al., 2008; Teem et al., 1993, 1996) and were assumed to stabilize the domain either alone or in combinations (1S, 3S, R, R1S, and R4S; see Figure 1B).
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ABCC7 p.Phe409Leu 22265408:26:64
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PMID: 18417076 [PubMed] Cheung JC et al: "Molecular basis for the ATPase activity of CFTR."
No. Sentence Comment
107 The construct generated had several mutations to increase solubility of the domain (F409L, F429S, F433L, G550E, R553Q, R555K, H667R) in addition to the deletion of F508.
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ABCC7 p.Phe409Leu 18417076:107:85
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PMID: 23378596 [PubMed] Hunt JF et al: "Cystic fibrosis transmembrane conductance regulator (ABCC7) structure."
No. Sentence Comment
164 (This mutation set is found in combination with the F409L, F429S, F433L, and H667R mutations in PDB IDs 1XMJ and 2BBO.)
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ABCC7 p.Phe409Leu 23378596:164:52
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236 Note that the structures shown here contain seven point mutations included in hNBD1 constructs because of their beneficial influence on yield during purification-F409L, F429S, F433L, G550E, R553Q, R555K, and H667R.
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ABCC7 p.Phe409Leu 23378596:236:162
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PMID: 24513531 [PubMed] Moran O et al: "On the structural organization of the intracellular domains of CFTR."
No. Sentence Comment
1241 However, as the native preparation of NBD1 and NBD2 tend to precipitate at relatively low concentration (>2.5 mg/ml; Galeno et al., 2011; Galfr&#e8; et al., 2012), to obtain protein concentrations compatible with the crystallization conditions, three to seven revertant mutations (F409L, F429S, F433L, G550E, R553Q, R555K, H667R, Roxo-Rosa et al., 2006; F429S, F494N, Q637R, Pissarra et al., 2008) have been introduced into the NBD1.
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ABCC7 p.Phe409Leu 24513531:1241:281
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