ABCB1 p.Leu1031Met
| Predicted by SNAP2: | A: N (57%), C: N (82%), D: D (75%), E: D (59%), F: N (93%), G: N (53%), H: N (61%), I: N (82%), K: N (53%), M: N (78%), N: N (53%), P: D (66%), Q: N (61%), R: D (59%), S: N (61%), T: N (72%), V: N (82%), W: D (63%), Y: N (72%), |
| Predicted by PROVEAN: | A: N, C: N, D: D, E: D, F: N, G: D, H: N, I: N, K: D, M: N, N: D, P: D, Q: D, R: D, S: N, T: N, V: N, W: N, Y: N, |
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[hide] Characterization of the ATPase activity of human A... In Vivo. 2005 Jul-Aug;19(4):657-60. Beljanski V, Soulika A, Tucker JM, Townsend DM, Davis W Jr, Tew KD
Characterization of the ATPase activity of human ATP-binding cassette transporter-2 (ABCA2).
In Vivo. 2005 Jul-Aug;19(4):657-60., [PMID:15999530]
Abstract [show]
BACKGROUND: ABCA2 is a member of the ATP binding cassette transporter family with functional roles in cholesterol homeostasis and drug resistance. MATERIALS AND METHODS: In order to characterize its ATPase activity, we transfected HEK293 cells with an ABCA2 mammalian expression system and isolated ABCA2-enriched membranes. RESULTS: We found no measurable ATPase activity of ABCA2 in isolated membranes, except in the presence of the methyl-beta-cyclodextrin. However, competitive binding of a pseudo-substrate, 8-azido-[alpha-32P]-ATP, was demonstrated. CHO cells transfected with ABCA2 did not have a higher rate of endogenous ATP hydrolysis when compared to the mock-transfected cells. CONCLUSION: Overall, we conclude that, while ABCA2 may have low levels of ATPase activity that can be substrate-stimulated, it is more likely to have a regulatory role in cell physiology.
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No. Sentence Comment
29 Mutations of the conserved lysine to methionine in the Walker A motif of the two nucleotide binding domains (L1031M and L2094M) were described elsewhere (15).
X
ABCB1 p.Leu1031Met 15999530:29:109
status: NEW