Cystic Fibrosis Transmembrane Conductance Regulator (ABCC7) Structure

被引：39

作者：

Hunt, John F. ^{[1
]}

Wang, Chi ^{[1
]}

Ford, Robert C. ^{[2
]}

机构：

[1] Columbia Univ, Dept Biol Sci, New York, NY 10027 USA

[2] Univ Manchester, Fac Life Sci, Manchester M13 9PT, Lancs, England

来源：

COLD SPRING HARBOR PERSPECTIVES IN MEDICINE | 2013年 / 3卷 / 02期

关键词：

ATP-BINDING CASSETTE; MEMBRANE H+-ATPASE; NUCLEOTIDE-BINDING; P-GLYCOPROTEIN; CHLORIDE CHANNEL; CRYSTAL-STRUCTURE; DELTA-F508; MUTATION; MOLTEN GLOBULE; SUBUNIT INTERACTIONS; MALTOSE TRANSPORTER;

D O I：

10.1101/cshperspect.a009514

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

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.

引用

页数：29

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