Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding

Journal of Biological Chemistry

Volumn 278, Issue 10, 2003, Pages 8294-8299

  Rosenberg, Mark F ^a   Kamis, Alhaji Bukar ^a   Callaghan, Richard ^b   Higgins, Christopher F ^c   Ford, Robert C ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOTHERAPY; CONFORMATIONS; CRYSTAL STRUCTURE; CRYSTALS; DRUG PRODUCTS;

MULTIDRUG RESISTANCE;

PROTEINS;

ABC TRANSPORTER; GLYCOPROTEIN P; MULTIDRUG RESISTANCE PROTEIN; NUCLEOTIDE BINDING PROTEIN; ADENOSINE TRIPHOSPHATE;

ALPHA HELIX; ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALLOGRAPHY; HYDROLYSIS; HYDROPHOBICITY; IMAGE ANALYSIS; LIPID BILAYER; MEMBRANE TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN STRUCTURE; ANIMAL; CHEMISTRY; CHO CELL; HAMSTER; METABOLISM; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

ANIMALIA; MAMMALIA;

ADENOSINE TRIPHOSPHATE; ANIMALS; CHO CELLS; CRICETINAE; CRYSTALLOGRAPHY, X-RAY; P-GLYCOPROTEIN; PROTEIN CONFORMATION;

EID: 0037424343     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M211758200     Document Type: Article

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