ABCMdb

ABCC7 p.His1402Ala

None has been submitted yet.

Publications

PMID: 11022033 [PubMed] Gentzsch M et al: "Localization of sequences within the C-terminal domain of the cystic fibrosis transmembrane conductance regulator which impact maturation and stability."

No. Sentence Comment

40 F1413A/ L1414A/V1415A/I1416A/E1417A, 5Ј-GCTGGAATGCCAACAAGCTGC- GGCCGCAGCAGAGAACAAAGTGCGG-3Ј and 5Ј-CCGCACTTTGTTC- TCTGCTGCGGCCGCAGCTTGTTGGCATTCCAGC-3Ј; F1413A- /L1414A/V1415A/I1416A, 5Ј-GCTGGAATGCCAACAAGCTGCGGCCG- CAGAAGAGAACAAAGTGCGG-3Ј and 5Ј-CCGCACTTTGTTCTCTTC- TGCGGCCGCAGCTTGTTGGCATTCCAGC-3Ј; Q1411A/Q1412A, 5Ј-G- GATAGAAGCAATGCTGGAATGCGCAGCATTTTTGGTCATAGAAG-3 and 5Ј-CTTCTATGACCAAAAATGCTGCGCATTCCAGCATTGCTTCT- ATCC-3; F1413A/L1414A, 5Ј-GCTGGAATGCCAACAAGCTGCGGTCA- TAGAAGAGAACAAAGTGCG-3Ј and 5Ј-CGCACTTTGTTCTCTTCTA- TGACCGCAGCTTGTTGGCATTCCAGC-3Ј; L1414A/V1415A, 5Ј-GCT- GGAATGCCAACAATTTGCGGCCATAGAAGAGAACAAAGTGCGG-3Ј and 5Ј-CCGCACTTTGTTCTCTTCTATGGCCGCAAATTGTTGGCATT- CCAGC-3Ј; V1415A/I1416A, 5Ј-GGAATGCCAACAATTTTTGGCCGCA- GAAGAGAACAAAGTGCGGCAG-3Ј and 5Ј-CTGCCGCACTTTGTTCT- CTTCTGCGGCCAAAAATTGTTGGCATTCC-3Ј; E1417A/E1418A, 5Ј- GCCAACAATTTTTGGTCATAGCAGCGAACAAAGTGCGGCAGTAC- G-3Ј and 5Ј-CGTACTGCCGCACTTTGTTCGCTGCTATGACCAAAAA- TTGTTGGC-3Ј; F1413A, 5Ј-GCAATGCTGGAATGCCAACAAGCTTTG- GTCATAGAAGAGAAC-3Ј and 5Ј-GTTCTCTTCTATGACCAAAGCTT- GTTGGCATTCCAGCATTGC-3Ј; L1414A, 5Ј-GCTGGAATGCCAACAA- TTTGCGGTCATAGAAGAGAACAAAGTGCG-3Ј and 5Ј-CGCACTTTG- TTCTCTTCTATGACCGCAAATTGTTGGCATTCCAGC-3Ј; V1415A, 5Ј- GGAATGCCAACAATTTTTGGCCATAGAAGAGAACAAAGTGCGGC- AG-3Ј and 5Ј-CTGCCGCACTTTGTTCTCTTCTATGGCCAAAAATTGT- TGGCATTCC-3Ј; I1416A, 5Ј-GGAATGCCAACAATTTTTGGTCGCAG- AAGAGAACAAAGTGCGGCAG-3Ј and 5Ј-CTGCCGCACTTTGTTCTC- TTCTGCGACCAAAAATTGTTGGCATTCC-3Ј; E1417A, 5Ј-GCCAACA- ATTTTTGGTCATAGCAGAGAACAAAGTGCGGCAGTACG-3Ј and 5Ј- CGTACTGCCGCACTTTGTTCTCTGCTATGACCAAAAATTGTTGGC- 3Ј; C1400A/E1401A/H1402A/R1403A/I1404A, 5Ј-GCACAGTAATTCTC- GCTGCAGCCGCGGCAGAAGCAATGCTGGAATGCC-3Ј and 5Ј-GGC- ATTCCAGCATTGCTTCTGCCGCGGCTGCAGCGAGAATTACTGTG- C-3Ј; ⌬1400-1404: 5Ј-GCATTTGCTGATTGCACAGTAATTCTCGAAG- CAATGCTGGAATGCC-3Ј and 5Ј-GGCATTCCAGCATTGCTTCGAGA- ATTACTGTGCAATCAGCAAATGC-3Ј; C1400A/E1401A, 5Ј-GATTGC- ACAGTAATTCTCGCTGCACACAGGATAGAAGCAATGC-3Ј and 5Ј-G- CATTGCTTCTATCCTGTGTGCAGCGAGAATTACTGTGCAATC-3Ј; H1402A/R1403A, 5Ј-CAGTAATTCTCTGTGAAGCCGCGATAGAAGC- AATGCTGGAATGCC-3Ј and 5Ј-GGCATTCCAGCATTGCTTCTATCG- CGGCTTCACAGAGAATTAC TG-3Ј; I1404A/E1405A, 5Ј-CTCTGTGA- ACACAGGGCAGCAGCAATGCTGGAATGCCAAC-3Ј and 5Ј-GTTGGC- ATTCCAGCATTGCTGCTGCCCTGTGTTCACAGAG-3Ј, Q1390A/A- 1391A/F1392A/A1393A/D1394A, 5Ј-GAAGAACTCTAAAAGCAGCAG- CTGCTGCTTGCACAGTAATTCTC-3Ј and 5Ј-GAGAATTACTGTGCA- AGCAGCAGCTGCTGCTTTTAGAGTTCTTC-3Ј. Login to comment

PMID: 12084728 [PubMed] Milewski MI et al: "Aggregation of misfolded proteins can be a selective process dependent upon peptide composition."

No. Sentence Comment

90 Only 25% (52/208) of cells expressing GFP fusion protein bearing single H1402A substitution and 27% (41/153) of R1403A mutants showed intracellular protein accumulation, whereas the corresponding number for the wild type sequence was 91% (132/145). Login to comment
93 Cells expressing the double mutant H1402A,R1403A showed no aggregation at all (0/108). Login to comment
97 However, the introduction of the ⌬ag deletion or the H1402A,R1403A double mutation significantly decreased the amount of the fusion protein in the insoluble fraction to approximately 31 and 36%, respectively. Login to comment
108 B-E, the effect of different mutations within the ag region, including ⌬ag (B), V1397E (C), T1396A (D), and double mutation H1402A,R1403A (E) on the aggregation of C terminus of CFTR fused to GFP (shown in green) in transiently transfected human airway epithelial (IB3-1) cells. Login to comment
120 Additionally, the double mutation H1402A,R1403A prevented aggregation of HA-tagged CFTR C terminus (Fig. 2E). Login to comment
146 E, lack of aggregation of HA-CFTR 1370-1480 construct carrying the H1402A and R1403A mutations. Login to comment
160 Similarly, the non-aggregating GFP-CFTR 1370-1480 H1402A,R1403A construct was included in giant aggregates formed by HA-CFTR 1370-1480 (Fig. 4D). Login to comment
195 C, colocalization of the aggregating GFP-CFTR 1370-1480 construct (green) and the non-aggregating HA-CFTR 1370-1480 H1402A,R1403A construct (red) in giant aggregates. Login to comment
196 D, co-localization of the non-aggregating GFP-CFTR 1370-1480 H1402A,R1403A construct (green) with the aggregating HA-CFTR 1370-1480 construct (red) in giant aggregates. Login to comment

PMID: 20110677 [PubMed] Kloch M et al: "The H-loop in the second nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator is required for efficient chloride channel closing."

No. Sentence Comment

30 Mutations within the H-loop of NBD2, including the deletion of the entire ag region (Δ1395-1403) and the double alanine substitution H1402A, R1403A (HR→AA), were created in the CFTR-containing pBQ4.7 vector (a gift from J. Rommens and L.-C. Tsui) using the site-directed mutagenesis system "Transformer" (Becton Dickinson). Login to comment

PMID: 15642363 [PubMed] Milewski MI et al: "PDZ-binding motifs are unable to ensure correct polarized protein distribution in the absence of additional localization signals."

No. Sentence Comment

25 Also, the introduction of the H1402A and R1403A mutations, reducing the aggregation rate of the CFTR C-terminus, was previously described [9]. Login to comment
64 A diagram illustrating the structure and subcellular localization of the GFP fusion proteins containing either the full-length CFTR protein or its C-terminal fragment (a.a. 1370-1480) with two alanine substitutions (H1402A and R1403A), eliminating the aggregation of the CFTR C-terminus. Login to comment
93 (B) Apical localization of the GFP-CFTR 1370-1480 H1402A, R1403A fusion protein containing the C-terminal M-K-D-T-R-L> motif. Login to comment
94 (C) Predominant cytoplasmic distribution of the GFP-CFTR 1370-1480 H1402A, R1403A fusion protein containing the extended Q-K-E-TC-L> PDZ-binding motif of LET23. Login to comment

PMID: 23378596 [PubMed] Hunt JF et al: "Cystic fibrosis transmembrane conductance regulator (ABCC7) structure."

No. Sentence Comment

289 Improvements in the yield of soluble protein were obtained by introducing the hydrolytically inactivating H1402A mutation in ATPase active site of hNBD2 plus a series of "solubilizing" mutations on its surface (Q1280E/ Y1307N/W1310H/Q1411D) (X Zhao, S Atwell, JF Hunt, et al., unpubl.). Login to comment
291 The H1402A mutation as well as at least some of the "solubilizing" mutations seem likely to stabilize the native conformation of the domain thermodynamically, as observed for the solubilizing surface mutations that improved the stability and yield J.F. Hunt et al. 18 Cite this article as Cold Spring Harb Perspect Med 2012;3:a009514 www.perspectivesinmedicine.org by Cold Spring Harbor Laboratory Press at SEMMELWEIS UNIV OF MEDICINE on December 5, of preparations of hNBD1 (as described above). Login to comment
293 Nonetheless, indirect evidence supports the hypothesis that the H1402A mutation stabilizes hNBD2. Login to comment
295 Electrophysiological studies of the H1402A and E1371Q mutations in intact human CFTR support these inferences concerning catalytic geometry by showing that the H1402A (Kloch et al. 2010) and E1371Q (Vergani et al. 2005) mutations both greatly increase the lifetime of the open state of the CFTR chloride channel, presumably because they block ATP hydrolysis and stabilize ATP-sandwich heterodimer formed by hNBD1 and hNBD2. Login to comment
297 However, despite their similar influence on the gating properties of intact CFTR, the H1402A and E1371Q mutations have dramatically different effects on the stabilityand yield of hNBD2 during purification, with the first greatly improving yield compared to the second (X Zhao, S Atwell, JF Hunt, et al., unpubl.). Login to comment
298 In silico energetic calculations suggest that the H1402A mutation stabilizes isolated hNBD2 bound to Mg-ATP, while the E1371Q mutation destabilizes it (P Kumar, C Wang, JF Hunt, et al., unpubl.). Login to comment

PMID: 24191035 [PubMed] Bozoky Z et al: "Regulatory R region of the CFTR chloride channel is a dynamic integrator of phospho-dependent intra- and intermolecular interactions."

No. Sentence Comment

117 Q1411D; L1436D; and H1402A) designed by SGX Inc. We find similar patterns of R region binding to NBD2 as for NBD1 (Fig. 1E), identifying NBD2 as a direct binding partner for R region and implying that the NBDs have similar binding properties. Login to comment
239 The NBD2 domain of human CFTR (aa 1193-1445, Q1280E; Y1307N; Q1411D; H1402A; and L1436D), a construct with solubilizing mutations designed by SGX, Inc., was encoded on a pET-SUMO plasmid (Invitrogen). Login to comment