Back to Search Start Over

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

Authors :
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.
Source :
Biochemistry. April 25, 2006, Vol. 45 Issue 16, p5251, 10 p.
Publication Year :
2006

Abstract

The mutating amino acid 553 in TM5 of ABCG2, a well conserved residue corresponding to glycine 589 of the Drosophila white protein, disrupts the function and trafficking that implies a similar role in the dimerization of the human transporter is reported. The results reveal that glycine 553 is important for protein trafficking and are consistent with its involvement in ABCG2 homodimerization.

Details

Language :
English
ISSN :
00062960
Volume :
45
Issue :
16
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.147193160