ABCA3 p.Gly1221Val
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PMID: 16959783
[PubMed]
Matsumura Y et al: "Characterization and classification of ATP-binding cassette transporter ABCA3 mutants in fatal surfactant deficiency."
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Sentence
Comment
179
To address this, the effects of introducing hydroxyl groups or alteration of side-chain size on ATP hydrolysis activity were investigated by generating three site-directed mutants (G1221A, G1221V, and G1221T), which were stably expressed in HEK293 cells.
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ABCA3 p.Gly1221Val 16959783:179:189
status: NEW182 In the G1221A and G1221V mutant proteins, which have a hydrophobic side chain, vanadate-induced nucleotide trapping was decreased to 15 and 18% of that of wild-type protein, respectively (Fig. 6, A, lanes 5-8, and B).
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ABCA3 p.Gly1221Val 16959783:182:18
status: NEW201 A, 20,000 ϫ g membrane fraction prepared from HEK293 cells stably expressing wild-type (Wt) ABCA3-GFP (lanes 3 and 4), G1221A (lanes 5 and 6), G1221V (lanes 7 and 8), G1221T (lanes 9 and 10), G1221S (lanes 11 and 12), or untransfected HEK293 cells (lanes 1 and 2) was incubated with 10 M 8-azido-[␣-32 P]ATP in the absence (-) or presence (ϩ) of 0.4 mM orthovanadate (Vi) and 3 mM MgCl2 for 10 min at 37 °C. Proteins werephotoaffinity-labeledwithUVirradiationafterremovalofunboundATP, electrophoresed on SDS-PAGE (5%), and transferred to a PVDF membrane.
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ABCA3 p.Gly1221Val 16959783:201:149
status: NEW