DC Field | Value | Language |
---|---|---|
dc.contributor.author | KIM, YOUNGJIN | - |
dc.contributor.author | Chen, Jue | - |
dc.date.accessioned | 2019-04-07T18:51:39Z | - |
dc.date.available | 2019-04-07T18:51:39Z | - |
dc.date.created | 2019-03-08 | - |
dc.date.issued | 2018-02 | - |
dc.identifier.issn | 0036-8075 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/96059 | - |
dc.description.abstract | The multidrug transporter permeability (P)-glycoprotein is an adenosine triphosphate (ATP)-binding cassette exporter responsible for clinical resistance to chemotherapy. P-glycoprotein extrudes toxic molecules and drugs from cells through ATP-powered conformational changes. Despite decades of effort, only the structures of the inward-facing conformation of P-glycoprotein are available. Here we present the structure of human P-glycoprotein in the outward-facing conformation, determined by cryo-electron microscopy at 3.4-angstrom resolution. The two nucleotide-binding domains form a closed dimer occluding two ATP molecules. The drug-binding cavity observed in the inward-facing structures is reorientated toward the extracellular space and compressed to preclude substrate binding. This observation indicates that ATP binding, not hydrolysis, promotes substrate release. The structure evokes a model in which the dynamic nature of P-glycoprotein enables translocation of a large variety of substrates. | - |
dc.language | English | - |
dc.publisher | AMER ASSOC ADVANCEMENT SCIENCE | - |
dc.relation.isPartOf | SCIENCE | - |
dc.title | Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation. | - |
dc.type | Article | - |
dc.identifier.doi | 10.1126/science.aar7389 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | SCIENCE, v.359, no.6378, pp.915 - 919 | - |
dc.identifier.wosid | 000425752600045 | - |
dc.citation.endPage | 919 | - |
dc.citation.number | 6378 | - |
dc.citation.startPage | 915 | - |
dc.citation.title | SCIENCE | - |
dc.citation.volume | 359 | - |
dc.contributor.affiliatedAuthor | KIM, YOUNGJIN | - |
dc.identifier.scopusid | 2-s2.0-85041198308 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | NUCLEOTIDE-BINDING DOMAINS | - |
dc.subject.keywordPlus | MULTIDRUG-RESISTANCE | - |
dc.subject.keywordPlus | CATALYTIC CYCLE | - |
dc.subject.keywordPlus | DRUG-BINDING | - |
dc.subject.keywordPlus | MEMBRANE GLYCOPROTEIN | - |
dc.subject.keywordPlus | GLUTAMATE RESIDUES | - |
dc.subject.keywordPlus | ALTERNATING ACCESS | - |
dc.subject.keywordPlus | ABC TRANSPORTERS | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | HYDROLYSIS | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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