Article
Mutational analysis of threonine 402 adjacent to the GXXXG dimerization motif in transmembrane segment 1 of ABCG2.
Biochemistry - 16 Mar 2010
Polgar Orsolya, Ierano Caterina, Tamaki Akina, Stanley Bradford, Ward Yvona, Xia Di, Tarasova Nadya, Robey Robert W, Bates Susan E
Abstract excerpt
ABCG2 is an ATP-binding cassette half-transporter important in normal tissue protection, drug distribution, and excretion. ABCG2 requires homodimerization for function, though the mechanism for dimerization has not been elucidated. We conducted mutational analysis of threonine 402, three residues from the GXXXG motif in TM1, to study its potential role in ABCG2 dimerization (TXXXGXXXG). Single mutations to...
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