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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2002-5-3
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pubmed:abstractText |
ATP-binding cassette transporters are responsible for the uptake and efflux of a multitude of substances across both eukaryotic and prokaryotic membranes. Members of this family of proteins are involved in diverse physiological processes including antigen presentation, drug efflux from cancer cells, bacterial nutrient uptake and cystic fibrosis. In order to understand more completely the role of these multidomain transporters an integrated approach combining structural, pharmacological and biochemical methods is being adopted. Recent structural data have been obtained on the cytoplasmic, nucleotide-binding domains of prokaryotic ABC transporters. This review evaluates both these data and the conflicting implications they have for domain communication in ABC transporters. Areas of biochemical research that attempt to resolve these conflicts will be discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport Systems, Basic,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MalK protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/NUBP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RAD50 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/histidine permease, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
1561
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
47-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11988180-ATP-Binding Cassette Transporters,
pubmed-meshheading:11988180-Amino Acid Sequence,
pubmed-meshheading:11988180-Amino Acid Transport Systems, Basic,
pubmed-meshheading:11988180-Animals,
pubmed-meshheading:11988180-Bacterial Proteins,
pubmed-meshheading:11988180-Binding Sites,
pubmed-meshheading:11988180-Carrier Proteins,
pubmed-meshheading:11988180-DNA-Binding Proteins,
pubmed-meshheading:11988180-Dimerization,
pubmed-meshheading:11988180-Fungal Proteins,
pubmed-meshheading:11988180-Humans,
pubmed-meshheading:11988180-Models, Molecular,
pubmed-meshheading:11988180-Molecular Sequence Data,
pubmed-meshheading:11988180-Nucleotides,
pubmed-meshheading:11988180-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11988180-Sequence Alignment
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pubmed:year |
2002
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pubmed:articleTitle |
Structure and association of ATP-binding cassette transporter nucleotide-binding domains.
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pubmed:affiliation |
Nuffield Department of Clinical Laboratory Sciences, University of Oxford, Level 4, John Radcliffe Hospital, OX3 9DS, UK. kerrid@icrf.icnet.uk
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pubmed:publicationType |
Journal Article,
Comparative Study,
Review
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