Article
Mutational studies of G553 in TM5 of ABCG2: a residue potentially involved in dimerization.
Biochemistry - 25 Apr 2006
Polgar Orsolya, Ozvegy-Laczka Csilla, Robey Robert W, Morisaki Kuniaki, Okada Masaki, Tamaki Akina, Koblos Gabriella, Elkind N Barry, Ward Yvona, Dean Michael, Sarkadi Balazs, Bates Susan E
Abstract excerpt
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...
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