Structural flexibility of the linker region of human P-glycoprotein permits ATP hydrolysis and drug transport

Biochemistry

Volumn 37, Issue 39, 1998, Pages 13660-13673

  Hrycyna, Christine A ^a   Airan, Lisa E ^a,b   Germann, Ursula A ^a,c   Ambudkar, Suresh V ^a   Pastan, Ira ^a   Gottesman, Michael M ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b WASHINGTON UNIVERSITY   (United States)

^c VERTEX PHARMACEUTICALS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLYCOPROTEIN P;

ARTICLE; CELL MEMBRANE TRANSPORT; HUMAN; MOLECULAR DYNAMICS; MULTIDRUG RESISTANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

3T3 CELLS; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; AZIDES; BASE SEQUENCE; BIOLOGICAL TRANSPORT; CELL MEMBRANE; DRUG RESISTANCE, MULTIPLE; GENETIC VECTORS; HELA CELLS; HUMANS; HYDROLYSIS; IODINE RADIOISOTOPES; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, INSERTIONAL; OSTEOSARCOMA; P-GLYCOPROTEIN; PEPTIDE FRAGMENTS; PRAZOSIN; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE DELETION; TUMOR CELLS, CULTURED; VERAPAMIL;

MAMMALIA; VACCINIA; VACCINIA VIRUS;

EID: 0032578434     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9808823     Document Type: Article

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