Abstract
Structural studies of the cystic fibrosis transmembrane conductance regulator (CFTR) are reviewed. Like many membrane proteins, full-length CFTR has proven to be difficult to express and purify, hence much of the structural data available is for the more tractable, independently expressed soluble domains. Therefore, this chapter covers structural data for individual CFTR domains in addition to the sparser data available for the full-length protein. To set the context for these studies, we will start by reviewing structural information on model proteins from the ATP-binding cassette (ABC) transporter superfamily, to which CFTR belongs.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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ATP-Binding Cassette Transporters / chemistry
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Crystallization
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Cystic Fibrosis Transmembrane Conductance Regulator / chemistry*
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GTP-Binding Proteins / chemistry
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Humans
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins / chemistry
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Mutation / genetics
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Protein Folding
Substances
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ATP-Binding Cassette Transporters
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CFTR protein, human
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Carrier Proteins
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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NUBP1 protein, human
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Cystic Fibrosis Transmembrane Conductance Regulator
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GTP-Binding Proteins