ABCB2 p.Val117Met
| Predicted by SNAP2: | A: N (93%), C: N (78%), D: N (61%), E: N (66%), F: N (82%), G: N (78%), H: N (78%), I: N (97%), K: N (72%), L: N (97%), M: N (87%), N: N (72%), P: N (87%), Q: N (82%), R: N (72%), S: N (87%), T: N (87%), W: D (66%), Y: N (78%), |
| Predicted by PROVEAN: | A: N, C: N, D: D, E: N, F: N, G: N, H: N, I: N, K: N, L: N, M: N, N: N, P: N, Q: N, R: D, S: N, T: N, W: D, Y: N, |
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[hide] ATP-binding-cassette (ABC) transport systems: func... FEMS Microbiol Rev. 1998 Apr;22(1):1-20. Schneider E, Hunke S
ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains.
FEMS Microbiol Rev. 1998 Apr;22(1):1-20., [PMID:9640644]
Abstract [show]
Members of the superfamily of adenosine triphosphate (ATP)-binding-cassette (ABC) transport systems couple the hydrolysis of ATP to the translocation of solutes across a biological membrane. Recognized by their common modular organization and two sequence motifs that constitute a nucleotide binding fold, ABC transporters are widespread among all living organisms. They accomplish not only the uptake of nutrients in bacteria but are involved in diverse processes, such as signal transduction, protein secretion, drug and antibiotic resistance, antigen presentation, bacterial pathogenesis and sporulation. Moreover, some human inheritable diseases, like cystic fibrosis, adrenoleukodystrophy and Stargardt's disease are caused by defective ABC transport systems. Thus, albeit of major significance, details of the molecular mechanism by which these systems exert their functions are still poorly understood. In this review, recent data concerning the properties and putative role of the ATP-hydrolyzing subunits/domains are summarized and compared between bacterial and eukaryotic systems.
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No. Sentence Comment
1529 Suppressor mutations in malK that restored transport of these mutants were found to map mainly in the helical domain of the MalK protein (A85M, V117M) [89], close to those residues which when mutated allowed LacK to substitute more e&#a4;ciently for MalK in maltose transport [92].
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ABCB2 p.Val117Met 9640644:1529:144
status: NEW