Mutational studies of G553 in TM5 of ABCG2: a residue potentially involved in dimerization.

@article{Polgar2006MutationalSO,
  title={Mutational studies of G553 in TM5 of ABCG2: a residue potentially involved in dimerization.},
  author={Orsolya Polgar and Csilla Ozvegy-Laczka and Robert W. Robey and Kuniaki Morisaki and Masaki Okada and Akina Tamaki and Gabriella Koblos and N. Barry Elkind and Yvona Ward and M. Dean and Bal{\'a}zs Sarkadi and Susan E Bates},
  journal={Biochemistry},
  year={2006},
  volume={45 16},
  pages={5251-60}
}
ABCG2 is an ATP-binding cassette half-transporter conferring resistance to chemotherapeutic agents such as mitoxantrone, irinotecan, and flavopiridol. With its one transmembrane and one ATP-binding domain, ABCG2 is thought to homodimerize for function. One conserved region potentially involved in dimerization is a three-amino acid sequence in transmembrane segment 5 (residues 552-554). Mutations in the corresponding residues in the Drosophila white protein (an orthologue of ABCG2) are thought… CONTINUE READING
12 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 12 extracted citations

Similar Papers

Loading similar papers…