ABCMdb

ABCC7 p.His667Arg

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Publications

PMID: 16697012 [PubMed] Ramaen O et al: "Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site."

No. Sentence Comment

63 Structure based sequence alignment of MRP1-NBD1 with MRP1-NBD2, h-CFTR-NBD1 (pdb code 1xmi, F508A F429S H667R mutant), BtuCD (pdb code 1l7v), TAP1 (pdb code 1jj7), MJ0796 (pdb code 1l2t, E171Q mutant), MJ1267 (pdb code 1g9x, N31C mutant), HisP (pdb code 1b0u) and HlyB-NBD (pdb code 1mt0). Login to comment

PMID: 11331356 [PubMed] Button B et al: "PKC-mediated stimulation of amphibian CFTR depends on a single phosphorylation consensus site. insertion of this site confers PKC sensitivity to human CFTR."

No. Sentence Comment

34 The 8-Br-cAMP-activated currents in the mutant H667R-hCFTR were very high; thus, cRNA injection was reduced to 1-2.5 ng/oocyte. Login to comment
74 For construction of the H667R-hCFTR mutant, the primer used was 5Ј-AGACCTTGCGCCGTTTCTCA-3Ј (construct screened with HhaI, underlined). Login to comment
228 Since Thr665 is present in hCFTR, we decided to determine whether the formation of a PKC consensus phosphorylation site in hCFTR by substituting His with Arg at position 667 is sufficient to confer the Xenopus phenotype to hCFTR. Login to comment
229 The mutant H667R-hCFTR was expressed in Xenopus oocytes and tested for activation by PKC stimulation. Login to comment
254 Insertion of this site in the H667R-hCFTR mutant resulted in a large increase in current in response to PKC activation. Login to comment
256 In any event, the results indicate that the PKC consensus phosphorylation site that includes Thr665 is critical for the response to PMA. If the activation of the H667R-hCFTR mutant is in fact less than that of the HXH chimera, then one would conclude also that the phosphorylation of Thr665, or its functional effect, involves other residues of the R domain of CFTR. Login to comment
274 PMA produces a large increase in conductance in a mutant hCFTR (H667R-hCFTR) with an engineered PKC consensus phosphorylation sequence that includes Thr665. Login to comment
275 (A) Representative I-V plot from an oocyte expressing H667R-hCFTR. Login to comment

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

82 Crystal Structure of hNBD1 Shows That Regulatory Protein Segments Adopt Multiple Conformations Altering Access to the Active Site-High-resolution diffraction data were obtained for hNBD1-2b-F508A, containing two solubilizing mutations (F429S and H667R) in addition to the F508A substitution (Table II). Login to 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). Login to comment
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. Login to comment

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. Login to comment

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]. Login to comment
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]. Login to comment

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

305 Equivalent structural analyses conducted on the F494N, Q637R, and H667R solubilizing mutations are described in detail in sections ST13-14 in the Supplementary Information. Login to comment

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). Login to comment

PMID: 20952391 [PubMed] Wang G et al: "State-dependent regulation of cystic fibrosis transmembrane conductance regulator (CFTR) gating by a high affinity Fe3+ bridge between the regulatory domain and cytoplasmic loop 3."

No. Sentence Comment

135 In addition, H667R, H775T, and H784Q but not Cys-832 and Asp-836 are found in the R domain of the mouse CFTR channel (Fig. 4A), which was found insensitive to Fe3ϩ (Fig. 4C). Login to comment

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). Login to comment

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. Login to comment

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.) Login to comment
165 The other mutation sets that improved the yield of soluble hNBD1 involved substitution of surface-exposed residues in hNBD1 with more polar residues occurring at the same position in CFTR orthologs from other species (F429S/F494N/ Q637R found in PDB ID 2BBS, F494N/ Q637R found in PDB ID 2BBT, and F429S/ H667R found in PDB ID 1XMI). Login to comment
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. Login to comment

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. Login to comment