Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 283, Issue 5, Pages 2939-2948Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M706645200
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Funding
- British Heart Foundation [PG/07/076/23480] Funding Source: Medline
- Cancer Research UK Funding Source: Medline
- NIAAA NIH HHS [T32 AA 07463] Funding Source: Medline
- NIDCR NIH HHS [DE 14765] Funding Source: Medline
- NIDDK NIH HHS [DK 54568, DK 34804] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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Specific residues in the putative pore helix, selectivity filter, and S6 transmembrane helix of the inositol 1,4,5-trisphosphate receptor were mutated in order to examine their effects on channel function. Mutation of 5 of 8 highly conserved residues in the pore helix/selectivity filter region inactivated the channel (C2533A, G2541A, G2545A, G2546A, and G2547A). Of the remaining three mutants, C2527A and R2543A were partially active and G2549A behaved like wild type receptor. Mutation of a putative glycine hinge residue in the S6 helix (G2586A) or a putative gating residue at the cytosolic end of S6 helix (F2592A) had minimal effects on function, although channel function was inactivated by G2586P and F2592D mutations. The mutagenesis data are interpreted in the context of a structural homology model of the inositol 1,4,5-trisphosphate receptor.
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