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Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
Published on: May 10, 2014
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CFTR structure and cystic fibrosis.
Natasha Cant1, Naomi Pollock1, Robert C Ford1
1University of Manchester, Faculty of Life Sciences, Michael Smith Building, Manchester M13 9PT, UK.
The International Journal of Biochemistry & Cell Biology
|February 19, 2014
Summary
Cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel protein. This review examines CFTR structure and function, comparing it to other ATP-binding cassette proteins and discussing methods for high-resolution structural determination.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ATP-binding cassette (ABC) transporter superfamily.
- Unlike most ABC proteins that function as transporters, CFTR acts as a channel with specific permeability to anions, particularly chloride and bicarbonate ions.
Purpose of the Study:
- To review the known structure and function of CFTR.
- To contextualize CFTR within the broader family of ATP-binding cassette proteins.
- To discuss current approaches for determining the high-resolution structure of CFTR.
Main Methods:
- Literature review of existing studies on CFTR structure and function.
- Comparative analysis of CFTR with other ATP-binding cassette proteins.
- Overview of structural biology techniques applied to CFTR.
Main Results:
- CFTR exhibits distinct channel activity, differing from the typical transporter function of most ABC proteins.
- Understanding CFTR's unique role provides insights into anion transport mechanisms.
- Various strategies are being employed to achieve high-resolution structural data for CFTR.
Conclusions:
- CFTR represents an atypical member of the ABC protein family, functioning as an anion channel.
- Further structural studies are crucial for a comprehensive understanding of CFTR's mechanism of action.
- Investigating CFTR's structure-function relationship can inform therapeutic strategies for related diseases.
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