As an ion channel, the cystic fibrosis transmembrane conductance regulator (CFTR) protein occupies a unique niche within the ABC family. Orthologues of CFTR are extant throughout the animal kingdom from sharks to platypods to sheep, where the osmoregulatory function of the protein has been applied to differing lifestyles and diverse organ systems. In humans, loss-of-function mutations to CFTR cause the disease cystic fibrosis, which is a significant health burden in populations of white European descent. Orthologue screening has proved fruitful in the pursuit of high-resolution structural data for several membrane proteins, and we have applied some of the princples developed in previous studies to the expression and purification of CFTR. We have overexpressed this protein, along with evolutionarily diverse orthologues, in Saccharomyces cerevisiae and developed a purification to isolate it in quantities sufficient for structural and functional studies.
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October 2015
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Review Article|
October 09 2015
Characterizing diverse orthologues of the cystic fibrosis transmembrane conductance regulator protein for structural studies
Naomi L. Pollock;
Naomi L. Pollock
*Faculty of Life Sciences, University of Manchester, Manchester M13 9PL, U.K.
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Tracy L. Rimington;
Tracy L. Rimington
*Faculty of Life Sciences, University of Manchester, Manchester M13 9PL, U.K.
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Robert C. Ford
Robert C. Ford
1
*Faculty of Life Sciences, University of Manchester, Manchester M13 9PL, U.K.
1To whom correspondence should be addressed (emailRobert.ford@manchester.ac.uk).
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Publisher: Portland Press Ltd
Received:
June 01 2015
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2015 Authors; published by Portland Press Limited
2015
Biochem Soc Trans (2015) 43 (5): 894–900.
Article history
Received:
June 01 2015
Citation
Naomi L. Pollock, Tracy L. Rimington, Robert C. Ford; Characterizing diverse orthologues of the cystic fibrosis transmembrane conductance regulator protein for structural studies. Biochem Soc Trans 1 October 2015; 43 (5): 894–900. doi: https://doi.org/10.1042/BST20150081
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