P-glycoprotein structure and evolutionary homologies
Identifieur interne : 002805 ( Main/Exploration ); précédent : 002804; suivant : 002806P-glycoprotein structure and evolutionary homologies
Auteurs : Irene Bosch [États-Unis] ; James M. Croop [États-Unis]Source :
- Cytotechnology [ 0920-9069 ] ; 1998-09-01.
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Abstract
Abstract: Analysis of multidrug resistant cell lines has led to the identification of the P-glycoprotein multigene family. Two of the three classes of mammalian P-glycoproteins have the ability to confer cellular resistance to a broad range of structurally and functionally diverse cytotoxic agents. P-glycoproteins are integral membrane glycoproteins comprised of two similar halves, each consisting of six membrane spanning domains followed by a cytoplasmic domain which includes a nucleotide binding fold. The P-glycoprotein is a member of a large superfamily of transport proteins which utilize ATP to translocate a wide range of substrates across biological membranes. This superfamily includes transport complexes comprised of multicomponent systems, half P-glycoproteins and P-glycoprotein-like homologs which appear to require approximately 12 α-helical transmembrane domains and two nucleotide binding folds for substrate transport. P-glycoprotein homologs have been isolated and characterized from a wide range of species. Amino acid sequences, the similarities between the halves and intron/exon boundaries have been compared to understand the evolutionary origins of the P-glycoprotein.
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DOI: 10.1023/A:1008080911522
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Croop</name><affiliation wicri:level="2"><country xml:lang="fr" wicri:curation="lc">États-Unis</country><wicri:regionArea>The Section of Pediatric Hematology/Oncology, James Whitcomb Riley Hospital for Children, Indiana University, 46202, Indianapolis, IN</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Cytotechnology</title><title level="j" type="sub">International Journal of Cell Culture and Biotechnology</title><title level="j" type="abbrev">Cytotechnology</title><idno type="ISSN">0920-9069</idno><idno type="eISSN">1573-0778</idno><imprint><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><date type="published" when="1998-09-01">1998-09-01</date><biblScope unit="volume">27</biblScope><biblScope unit="issue">1-3</biblScope><biblScope unit="page" from="1">1</biblScope><biblScope unit="page" to="30">30</biblScope></imprint><idno type="ISSN">0920-9069</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0920-9069</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ABC transporters</term><term>MDR</term><term>P-glycoprotein</term><term>multidrug resistance</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Analysis of multidrug resistant cell lines has led to the identification of the P-glycoprotein multigene family. Two of the three classes of mammalian P-glycoproteins have the ability to confer cellular resistance to a broad range of structurally and functionally diverse cytotoxic agents. P-glycoproteins are integral membrane glycoproteins comprised of two similar halves, each consisting of six membrane spanning domains followed by a cytoplasmic domain which includes a nucleotide binding fold. The P-glycoprotein is a member of a large superfamily of transport proteins which utilize ATP to translocate a wide range of substrates across biological membranes. This superfamily includes transport complexes comprised of multicomponent systems, half P-glycoproteins and P-glycoprotein-like homologs which appear to require approximately 12 α-helical transmembrane domains and two nucleotide binding folds for substrate transport. P-glycoprotein homologs have been isolated and characterized from a wide range of species. Amino acid sequences, the similarities between the halves and intron/exon boundaries have been compared to understand the evolutionary origins of the P-glycoprotein.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Indiana</li><li>Massachusetts</li></region></list><tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Bosch, Irene" sort="Bosch, Irene" uniqKey="Bosch I" first="Irene" last="Bosch">Irene Bosch</name></region><name sortKey="Croop, James M" sort="Croop, James M" uniqKey="Croop J" first="James M." last="Croop">James M. Croop</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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