ABCC5 p.Phe343Arg
Predicted by SNAP2: | A: D (71%), C: N (61%), D: D (91%), E: D (85%), G: D (80%), H: D (80%), I: N (57%), K: D (85%), L: N (57%), M: N (61%), N: D (80%), P: D (91%), Q: D (75%), R: D (75%), S: D (75%), T: D (63%), V: D (53%), W: D (71%), Y: D (63%), |
Predicted by PROVEAN: | A: D, C: D, D: D, E: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, Q: D, R: D, S: D, T: D, V: D, W: D, Y: N, |
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[hide] Mutational analysis of ABC proteins. Arch Biochem Biophys. 2008 Aug 1;476(1):51-64. Epub 2008 Mar 5. Loo TW, Clarke DM
Mutational analysis of ABC proteins.
Arch Biochem Biophys. 2008 Aug 1;476(1):51-64. Epub 2008 Mar 5., [PMID:18328253]
Abstract [show]
The 49 human members of the ATP-binding cassette (ABC) family of proteins are involved in a wide range of activities such as active transport of compounds across membranes, extraction of compounds out of membranes, functioning as ion channels, or regulators of channel activity. Mutations and/or overexpression of many of the proteins can have adverse effects on health. A goal in the study of ABC proteins is to understand their mechanisms of action. This review will focus on the mutational approaches that have been used to study the structure and mechanisms of some ABC proteins.
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No. Sentence Comment
376 For example, the L65R, T199R and I306R mutations inhibited vinblastine interactions, the I306R and F343R changes inhibited binding of cyclosporin A and the F343R mutation inhibited binding of rhodamine.
X
ABCC5 p.Phe343Arg 18328253:376:99
status: NEWX
ABCC5 p.Phe343Arg 18328253:376:156
status: NEW