ABCC5 p.Phe335Cys
| Predicted by SNAP2: | A: N (53%), C: N (61%), D: D (85%), E: D (80%), G: D (53%), H: D (63%), I: N (66%), K: D (71%), L: N (82%), M: N (82%), N: D (75%), P: D (85%), Q: N (53%), R: D (71%), S: N (53%), T: N (53%), V: N (61%), W: D (71%), Y: N (61%), |
| Predicted by PROVEAN: | A: N, C: D, D: D, E: D, G: D, H: D, I: N, K: D, L: N, 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] 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
315 Seven TM6 cysteine mutants (V331C, T333C, F335C, S337C, L339C, G341C, F343C) were labeled in the presence or absence of AMPÁPNP or after vanadate trapping of nucleotide.
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ABCC5 p.Phe335Cys 18328253:315:42
status: NEW