The ABC transporter structure and mechanism: Perspectives on recent research

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dc.contributor.author Jones, PM
dc.contributor.author George, AM
dc.date.accessioned 2009-12-21T02:30:00Z
dc.date.issued 2004-03
dc.identifier.citation Cellular and Molecular Life Sciences, 2004, 61 (6), pp. 682 - 699
dc.identifier.issn 1420-682X
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/3730
dc.description.abstract ATP-binding cassette (ABC) transporters are multidomain integral membrane proteins that utilise the energy of ATP hydrolysis to translocate solutes across cellular membranes in all phyla. ABC transporters form one of the largest of all protein families and are central to many important biomedical phenomena, including resistance of cancers and pathogenic microbes to drugs. Elucidation of the structure and mechanism of ABC transporters is essential to the rational design of agents to control their function. While a wealth of high-resolution structures of ABC proteins have been produced in recent years, many fundamental questions regarding the protein's mechanism remain unanswered. In this review, we examine the recent structural data concerning ABC transporters and related proteins in the light of other experimental and theoretical data, and discuss these data in relation to current ideas concerning the transporters' molecular mechanism.
dc.language eng
dc.relation.isbasedon 10.1007/s00018-003-3336-9
dc.title The ABC transporter structure and mechanism: Perspectives on recent research
dc.type Journal Article
dc.parent Cellular and Molecular Life Sciences
dc.journal.volume 6
dc.journal.volume 61
dc.publocation Besel en_US
dc.identifier.startpage 682 en_US
dc.identifier.endpage 699 en_US
dc.cauo.name SCI.Environmental Sciences en_US
dc.conference Verified OK en_US
dc.for 0601 Biochemistry and Cell Biology
dc.personcode 020174
dc.personcode 860231
dc.percentage 100 en_US
dc.classification.name Biochemistry and Cell Biology en_US
dc.classification.type FOR-08 en_US
dc.description.keywords ABC transporter
dc.description.keywords ABC-ATPase
dc.description.keywords ATP hydrolysis
dc.description.keywords Mechanism
dc.description.keywords Membrane transport
dc.description.keywords Nucleotide-binding domain
dc.description.keywords P-glycoprotein
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - i3
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc true
utslib.collection.history Closed (ID: 3)
utslib.collection.history School of Medical and Molecular Sciences (ID: 341)


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