Article
Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to low affinity substrate binding state.
The Journal of biological chemistry - 14 Nov 2003
Zhang Da-Wei, Gu Hong-Mei, Situ Donna, Haimeur Anass, Cole Susan P C, Deeley Roger G
Abstract excerpt
Human multidrug resistance protein 1 (MRP1) confers resistance to many chemotherapeutic agents and transports diverse conjugated organic anions. We previously demonstrated that Glu1089 in transmembrane (TM) 14 is critical for the protein to confer anthracycline resistance. We have now assessed the functional importance of all polar and charged amino acids in this TM helix. Asn1100, Ser1097, and Lys1092, which are...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphate
- Amino Acid Motifs
- Amino Acid Sequence
- Amino Acids
- Animals
- Anions
- Asparagine
- Aspartic Acid
- Binding Sites