| Literature DB >> 23378596 |
John F Hunt1, Chi Wang, Robert C Ford.
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.Entities:
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Year: 2013 PMID: 23378596 PMCID: PMC3552343 DOI: 10.1101/cshperspect.a009514
Source DB: PubMed Journal: Cold Spring Harb Perspect Med ISSN: 2157-1422 Impact factor: 6.915