ABCMdb

PMID: 15159388

Tombline G, Bartholomew LA, Urbatsch IL, Senior AE
Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly.
J Biol Chem. 2004 Jul 23;279(30):31212-20. Epub 2004 May 24., 2004-07-23 [PubMed]

Sentences

No. Mutations Sentence Comment

48 ABCB1 p.Glu1201Gln ABCB1 p.Glu556Gln ABCB1 p.Glu1201Ala ABCB1 p.Glu556Ala Two such mutants have been reported, namely the E556Q/E1201Q and E556A/E1201A mutants of human Pgp (28). Login to comment 85 ABCB1 p.Glu556Gln We have found however that the mutations E556Q, E552A, or E1197Q in mouse MDR3 Pgp have no effect on the ability of the protein to undergo repeated cycles of Vi-induced trapping of ADP and release (G. Tombline, L. A. Bartholomew, I. L. Urbatsch, and A. E. Senior, manuscript in preparation). Login to comment 277 ABCB1 p.Glu1201Gln ABCB1 p.Glu1201Gln ABCB1 p.Glu556Gln ABCB1 p.Glu556Gln It may also be mentioned that Sauna et al. (28) found by UV-photolabeling and trypsin hydrolysis that the 8-azido-ADP occluded by the E556Q/E1201Q mutant of human Pgp after preincubation with 8-azido-ATP was distributed about equally in Nand C-halves of the protein, implying binding in both NBDs (the stoichiometry of bound nucleotide was not determined). Login to comment