ABCG2 p.Lys652Gln
| Predicted by SNAP2: | A: D (66%), C: D (63%), D: D (85%), E: D (80%), F: D (80%), G: D (80%), H: D (63%), I: D (66%), L: D (71%), M: D (71%), N: N (61%), P: D (71%), Q: N (53%), R: N (78%), S: D (66%), T: D (71%), V: D (66%), W: D (85%), Y: D (71%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: D, L: D, M: D, N: D, P: D, Q: D, R: N, S: D, T: D, V: D, W: D, Y: D, |
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[hide] Functional expression of the human breast cancer r... Biochem Biophys Res Commun. 2004 Jul 30;320(3):730-7. Mao Q, Conseil G, Gupta A, Cole SP, Unadkat JD
Functional expression of the human breast cancer resistance protein in Pichia pastoris.
Biochem Biophys Res Commun. 2004 Jul 30;320(3):730-7., 2004-07-30 [PMID:15240109]
Abstract [show]
We report functional expression of BCRP in Pichia pastoris in which BCRP was produced as a 62 kDa underglycosylated protein. BCRP expression level in P. pastoris was comparable to that in HEK cells. The basal BCRP ATPase activity in the yeast membranes was approximately 40-80 nmol Pi/min/mg protein, which can be modulated by known BCRP substrates and inhibitors. Photolabeling of BCRP with 8-azido[alpha-32P]ATP was dependent preferentially on the presence of Co2+ than Mg2+ and could be inhibited by a molar excess of ATP. Vanadate-induced trapping of 8-azido[alpha-32P]ADP by BCRP was much more significant in the presence of Co2+ than that with Mg2+. The Km and Vmax values of BCRP for [3H]E1S transport were 3.6+/-0.3 microM and 55.2+/-1.6 pmol/min/mg protein, respectively. This efficient and cost-effective expression system should facilitate large scale production and purification of BCRP for further structural and functional analyses.
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No. Sentence Comment
64 Except for a change of lysine at position 652 to glutamine, no other amino acid changes were introduced by PCR.
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ABCG2 p.Lys652Gln 15240109:64:23
status: VERIFIED