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Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation

Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2007528139

Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation

About this item

Full title

Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation

Author / Creator

Publisher

United States: The American Association for the Advancement of Science

Journal title

Science (American Association for the Advancement of Science), 2018-02, Vol.359 (6378), p.915-919

Language

English

Formats

Publication information

Publisher

United States: The American Association for the Advancement of Science

More information

Scope and Contents

Contents

Permeability glycoprotein (PgP) uses the energy from adenosine triphosphate (ATP) hydrolysis to transport substrates out of the cell. Many of its substrates are drugs, so it plays an important role in drug resistance. Structures in the inward-facing conformation have been determined for mouse, yeast, and algal PgP. Kim and Chen present the cryo–ele...

Alternative Titles

Full title

Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation

Authors, Artists and Contributors

Author / Creator

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_2007528139

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2007528139

Other Identifiers

ISSN

0036-8075

E-ISSN

1095-9203

DOI

10.1126/science.aar7389

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