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Updated: May 14, 2026
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Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
Published on: May 10, 2014
Cystic fibrosis transmembrane conductance regulator (ABCC7) structure
John F Hunt1, Chi Wang, Robert C Ford
1Department of Biological Sciences, Columbia University, New York, NY 10027, USA. jfhunt@biology.columbia.edu
Cold Spring Harbor Perspectives in Medicine
|February 5, 2013
Summary
Structural studies of cystic fibrosis transmembrane conductance regulator (CFTR) are challenging due to protein expression difficulties. Research focuses on individual CFTR domains and related ATP-binding cassette (ABC) transporters for insights.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Medicine
Background:
- Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) is a crucial membrane protein.
- Full-length CFTR is difficult to express and purify for structural studies.
- The ATP-binding cassette (ABC) transporter superfamily provides model systems for understanding CFTR.
Purpose of the Study:
- To review available structural data for CFTR.
- To discuss structural information on individual CFTR domains.
- To provide context using structural data from related ABC transporters.
Main Methods:
- Literature review of structural studies.
- Analysis of data for individual CFTR domains.
- Examination of structural data for ABC transporter superfamily members.
Main Results:
- Limited structural data exists for full-length CFTR.
- More extensive structural data is available for individual CFTR domains.
- Structural insights from homologous ABC transporters aid in understanding CFTR.
Conclusions:
- Structural studies of CFTR are ongoing and rely heavily on domain-specific data.
- Understanding CFTR structure is key to developing targeted therapies for cystic fibrosis.
- Comparative structural analysis within the ABC transporter superfamily is essential.
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