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CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains

CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2756053

CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains

About this item

Full title

CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2005-02, Vol.433 (7028), p.876-880

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

ABC (ATP-binding cassette) proteins constitute a large family of membrane proteins that actively transport a broad range of substrates. Cystic fibrosis transmembrane conductance regulator (CFTR), the protein dysfunctional in cystic fibrosis, is unique among ABC proteins in that its transmembrane domains comprise an ion channel. Opening and closing...

Alternative Titles

Full title

CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2756053

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2756053

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/nature03313

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