Structure and association of ATP-binding cassette transporter nucleotide-binding domains

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,...

Disgrifiad llawn

Manylion Llyfryddiaeth
Prif Awdur: Kerr, I
Fformat: Journal article
Iaith:English
Cyhoeddwyd: Elsevier 2002
Pynciau:
_version_ 1826267732212973568
author Kerr, I
author_facet Kerr, I
author_sort Kerr, I
collection OXFORD
description 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.
first_indexed 2024-03-06T20:58:42Z
format Journal article
id oxford-uuid:3a23b5d9-5b37-41cb-b24a-7de4222bd848
institution University of Oxford
language English
last_indexed 2024-03-06T20:58:42Z
publishDate 2002
publisher Elsevier
record_format dspace
spelling oxford-uuid:3a23b5d9-5b37-41cb-b24a-7de4222bd8482022-03-26T13:59:45ZStructure and association of ATP-binding cassette transporter nucleotide-binding domainsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3a23b5d9-5b37-41cb-b24a-7de4222bd848BiochemistryEnglishOxford University Research Archive - ValetElsevier2002Kerr, IATP-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.
spellingShingle Biochemistry
Kerr, I
Structure and association of ATP-binding cassette transporter nucleotide-binding domains
title Structure and association of ATP-binding cassette transporter nucleotide-binding domains
title_full Structure and association of ATP-binding cassette transporter nucleotide-binding domains
title_fullStr Structure and association of ATP-binding cassette transporter nucleotide-binding domains
title_full_unstemmed Structure and association of ATP-binding cassette transporter nucleotide-binding domains
title_short Structure and association of ATP-binding cassette transporter nucleotide-binding domains
title_sort structure and association of atp binding cassette transporter nucleotide binding domains
topic Biochemistry
work_keys_str_mv AT kerri structureandassociationofatpbindingcassettetransporternucleotidebindingdomains