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- W1607226074 abstract "The ABC superfamily of membrane transporters is one of the largest classes of proteins across all species and one of the most intensely researched. ABC proteins are involved in the trafficking of a diverse variety of biological molecules across cell membranes, with some members implicated in medical syndromes such as cystic fibrosis and multidrug resistance to anti‐cancer drugs. In the absence of X‐ray crystallographic data, structural information has come from spectroscopy, electron microscopy, secondary structure prediction algorithms and residue substitution, epitope labelling and cysteine cross‐linking studies. These have generally supported a model for the topology of the transmembrane domains of ABC transporters in which a single aqueous pore is formed by a toroidal ring of 12 α helices, deployed in two arcs of six helices each. Although this so‐called 6 + 6 helix model can be arranged in either mirror or rotational symmetry configurations, experimental data supports the former. In this review, we put forward arguments against both configurations of this 6 + 6 helix model, based on what is known generally about symmetry relationships in proteins. We relate these arguments to P‐glycoprotein, in particular, and discuss alternative models for the structure of ABC transporters in the light of the most recent research." @default.
- W1607226074 created "2016-06-24" @default.
- W1607226074 creator A5022673817 @default.
- W1607226074 creator A5042660265 @default.
- W1607226074 date "2000-09-01" @default.
- W1607226074 modified "2023-10-09" @default.
- W1607226074 title "Symmetry and structure in P-glycoprotein and ABC transporters" @default.
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- W1607226074 doi "https://doi.org/10.1046/j.1432-1327.2000.01628.x" @default.
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