Replacement of the positively charged Walker A lysine residue with a hydrophobic leucine residue and conformational alterations caused by this mutation in MRP1 impair ATP binding and hydrolysis

Biochemical Journal

Volumn 397, Issue 1, 2006, Pages 121-130

  Buyse, Frederic ^a   Hou, Yue Xian ^b   Vigano, Catherine ^a   Zhao, Qing ^b   Ruysschaert, Jean Marie ^a   Chang, Xiu Bao ^b  

^a UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^b MAYO CLINIC   (United States)

Author keywords

ATP binding hydrolysis; ATP dependent transport; Conformation; Multidrug resistance; Multidrug resistance protein 1 (MRP1); Nucleotide binding domain

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; CONFORMATIONS; HYDROLYSIS; HYDROPHOBICITY; PROTEINS;

ATP BINDING/HYDROLYSIS; ATP-DEPENDENT TRANSPORT; MULTIDRUG RESISTANCE; MULTIDRUG RESISTANCE PROTEIN 1 (MRP1); NUCLEOTIDE-BINDING DOMAINS;

AMINO ACIDS;

ADENOSINE TRIPHOSPHATE; ANTINEOPLASTIC AGENT; COLCHICINE; DAUNORUBICIN; EDETIC ACID; EGTAZIC ACID; LEUCINE; LYSINE; MULTIDRUG RESISTANCE PROTEIN 1; NUCLEOTIDE BINDING PROTEIN; PROTEIN K1333L; PROTEIN K684L; UNCLASSIFIED DRUG; VANADATE SODIUM; VERAPAMIL; VINCRISTINE; MULTIDRUG RESISTANCE PROTEIN; MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN 1;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; HYDROLYSIS; MULTIDRUG RESISTANCE; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT; WILD TYPE; ANIMAL; CELL CULTURE; CHEMISTRY; CYTOLOGY; GENETICS; HAMSTER; HYDROPHOBICITY; KIDNEY; METABOLISM; PHYSIOLOGY; SITE DIRECTED MUTAGENESIS; TRANSPORT AT THE CELLULAR LEVEL;

ADENOSINE TRIPHOSPHATE; ANIMALS; BIOLOGICAL TRANSPORT; CELLS, CULTURED; CRICETINAE; DRUG RESISTANCE, MULTIPLE; HYDROLYSIS; HYDROPHOBICITY; KIDNEY; LYSINE; MULTIDRUG RESISTANCE-ASSOCIATED PROTEINS; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY;

EID: 33745573710     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051363     Document Type: Article

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