ABCMdb

ABCC7 p.Lys464Met

None has been submitted yet.

Publications

PMID: 10951189 [PubMed] Duffieux F et al: "Nucleotide-binding domain 1 of cystic fibrosis transmembrane conductance regulator production of a suitable protein for structural studies."

No. Sentence Comment

40 Synthetic mutated oligonucleotides (Eurogentec) were K464M: 5H -CCACTGGAGCAGGCATGA- CTTCACTTCTAATGGTG-3H and D572M: 5H -GCTGATTTGT- ATTTATTAATGTCTCCTTTTGGATACC-3H , where underlined nucleotides represent mutations. Login to comment
116 Mutations were introduced in the Walker A and B motifs (K464M, D572M), at positions known to be involved in ATP binding and hydrolysis [21]. Login to comment

PMID: 9379898 [PubMed] Wemmie JA et al: "Mutational analysis of the Saccharomyces cerevisiae ATP-binding cassette transporter protein Ycf1p."

No. Sentence Comment

133 These mutants corresponded to CFTR alterations known to be associated with cystic fibrosis (G551D and G551S in CFTR, G756D and G756S in Ycf1p) as well as lesions that either disturb normal function (K464M in CFTR, K669M in Ycf1p) or act to suppress the phenotype of ⌬F508 CFTR (R553Q and R553M in CFTR, K758Q and K758M in CFTR). Login to comment
137 The analogous mutations in the CFTR are also non-functional but localized correctly, with the exception of the K464M mutant, which does not function normally and is apparently not properly targeted (Gregory et al., 1991). Login to comment
238 A mutation not associated with CF (K669M in Ycf1p, K464M in CFTR) produced a non-functional, vacuolar membrane-localized protein when present in Ycf1p but was apparently retained in the endoplasmic reticulum in the context of the CFTR (Gregory et al., 1991). Login to comment

PMID: 9711592 [PubMed] King SA et al: "Recombinant synthesis of cystic fibrosis transmembrane conductance regulator and functional nucleotide-binding domains."

No. Sentence Comment

191 For example, a glycine ~ aspartic acid replacement at CFTR position 551 within a highly conserved ABC protein motif (LSGGQXQR, glycine corresponding to position 551 underlined) disrupts the nucleotide interaction.5 The same appears to be true when a critical lysine residue in the Walker A site of NBD1 is substituted for methionine (K464M.) Login to comment
198 Maximal binding for the wild-type NBD1 was approximately four times that of the G551D and K464M domains. Login to comment

PMID: 1699669 [PubMed] Cheng SH et al: "Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis."

No. Sentence Comment

4 Examination of the various mutant proteins in COS-7 cells indicated that mature, fully glycosylated CFTR was absent from cells containing AF508, Al507, K464M, F506R, and S5491 cDNA plasmids. Login to comment
117 Analysis of Mutant Forms of CFTR Expression vectors containing wild-type CFTR (pMT-CFTR, lane 2) and those containing the mutants pMT-CFTR-K464M (lane 3) pMT-CFTR-K1250M (lane 4) pMT-CFTR-Al507 (lane 5) pMT-CFTR-N894. Login to comment
124 K464M cDNA transfected cells, like their Al507 and AF508 nucleotide binding domain 1 mutant counterparts, contain no band C (lane 3). Login to comment
137 CFTR Mutants Mutant CF Exon CFTR Domain A B C Wild type R334W K464M Al507 AF508 F508R s5491 G551 D N894,900Q K1250M Tthllll Y 7 N 9 Y 10 Y 10 N 10 Y 11 Y 11 N 15 N 20 N 22 TM6 NBDl NBDl NBDl NBDl NBDl NBDl ECD4 NBD2 Term - + ++ - + ++ - + - - + - - + - - + - - + - - + ++ + - - - + ++ - + - The known association with CF (Y, yes; N, no), exon localization, domain location, and presence (+ ) or absence (- ) of bands A, B, and C of mutant CFTR species is shown. Login to comment
179 We need to study the ability of these mutants to complement the chloride channel defect in CF epithelial cells to establish, for example, whether K1250M and K464M both abolish function. Login to comment