ABCC7 p.Glu504Gln
[switch to full view]Comments [show]
None has been submitted yet.
PMID: 12968023
[PubMed]
Orelle C et al: "The conserved glutamate residue adjacent to the Walker-B motif is the catalytic base for ATP hydrolysis in the ATP-binding cassette transporter BmrA."
No.
Sentence
Comment
39
To screen for positive clones, oligonucleotides were designed to introduce simultaneously a new AatII restriction site, without modifying the protein sequence, and the desired mutation: E504A, GTCGAGACTTGACGTC- GCTGCATCGAGCATAAG; E504Q, GTCGAGACTTGACGTCGCTTG- ATCGAGCATAAGA; E504C, GTCGAGACTTGACGTCGCACAATC- GAG CATAAGA; E504D, GTCGAGACTTGACGTCGCATCATCGAGC- ATAAG; and E504S, GTCGAGACTTGACGTCGCTGAATCGAGCATA- AGAA.
X
ABCC7 p.Glu504Gln 12968023:39:230
status: NEW78 The two other mutants, namely E504Q and especially E504A, might have an impaired ability to bind the ATP analogue, as further confirmed by increasing its concen- FIG. 1.
X
ABCC7 p.Glu504Gln 12968023:78:30
status: NEW109 Lane 1, wild-type BmrA; lane 2, E504A mutant; lane 3, E504C mutant; lane 4, E504D mutant; lane 5, E504Q mutant; and lane 6, E504S mutant.
X
ABCC7 p.Glu504Gln 12968023:109:98
status: NEW112 BmrA protein ATPase activity Hoechst transport nmol ATP hydrolyzed per min/mg protein Wild-type 6,500 Ϯ 500 ϩϩϩ E504D 0 Ϯ 5 - E504A 0 Ϯ 5 - E504C 0 Ϯ 5 ND E504Q 0 Ϯ 5 ND E504S 0 Ϯ 5 ND FIG. 3.
X
ABCC7 p.Glu504Gln 12968023:112:197
status: NEW169 However, addition of ATP in the presence of Mg2ϩ destroyed the ring-shaped structure not only for the wild-type BmrA but also for the E504Q mutant.
X
ABCC7 p.Glu504Gln 12968023:169:140
status: NEW
PMID: 9511935
[PubMed]
Bianchet MA et al: "Modeling of nucleotide binding domains of ABC transporter proteins based on a F1-ATPase/recA topology: structural model of the nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator (CFTR)."
No.
Sentence
Comment
226
Mutations such as E504Q do cause CF.
X
ABCC7 p.Glu504Gln 9511935:226:18
status: NEW257 Certainly, the disease causing mutation E504Q, and probably the AI507 and AF508 mutations have an effect on the function, position, and in the geometry of the loop that contains E504.
X
ABCC7 p.Glu504Gln 9511935:257:40
status: NEW360 The CFTR NBD1 model that results (Fig. 6) gathers the disease causing mutations in three different clusters: (1) mutations affecting the nucleotide binding pocket and the putative general base: A455E, G458V, E504Q AI507 AF508 P574H; (2) mutations in motif C which are probably related to an interaction with region D: S549[R,N,I] G551[S,D], R553Q; and (3) mutations within or near motif B, L558S, A559T, R560T, Y563N and mutations S492F and G480C.
X
ABCC7 p.Glu504Gln 9511935:360:208
status: NEW
PMID: 9511927
[PubMed]
Ko YH et al: "Frontiers in research on cystic fibrosis: understanding its molecular and chemical basis and relationship to the pathogenesis of the disease."
No.
Sentence
Comment
93
Consistent with the predicted functional importance of E504 as a catalytic base (see Discussion above), it will be noted that the inherited mutation E504Q also causes cystic fibrosis.
X
ABCC7 p.Glu504Gln 9511927:93:149
status: NEW
PMID: 7681034
[PubMed]
Ivaschenko TE et al: "Two new mutations detected by single-strand conformation polymorphism analysis in cystic fibrosis from Russia."
No.
Sentence
Comment
18
Actually only three new CF mutations have been detected in this country so far - 3821delT (White et al. 1991), 1677delTA (Ivaschenko et al. 1991), and E504Q (Baranov et al. 1991b).
X
ABCC7 p.Glu504Gln 7681034:18:151
status: NEW19 Two of them (1677delTA and E504Q) were found by chance as a by-product of exon 10 analysis for AF508 mutation in CF high-risk families requesting prenatal diagnosis.
X
ABCC7 p.Glu504Gln 7681034:19:27
status: NEW