ABCMdb

PMID: 9220975

Taguchi Y, Kino K, Morishima M, Komano T, Kane SE, Ueda K
Alteration of substrate specificity by mutations at the His61 position in predicted transmembrane domain 1 of human MDR1/P-glycoprotein.
Biochemistry. 1997 Jul 22;36(29):8883-9., 1997-07-22 [PubMed]

Sentences

No. Mutations Sentence Comment

8 ABCB1 p.His61Lys ABCB1 p.His61Phe We also showed that the replacement of His61 by Phe and Lys greatly impaired the efflux of calcein AM, while the replacement had no effect on the efflux of rhodamine 123. Login to comment 91 ABCB1 p.His61Phe ABCB1 p.His61Met The replacement of His61 by Phe, Met, or Trp, which has a nonpolar and bulkier side chain than His, reduced resistance to Vbl and increased resistance to Col, Adr, and VP16, resulting in a resistance order of Adr ≈ Col > Vbl ≈ VP16. Login to comment 92 ABCB1 p.His61Arg ABCB1 p.His61Lys The replacement of His61 by Lys or Arg, which have a bulkier and basic side chain, reduced resistance to Vbl and Adr and increased resistance to Col and VP16, resulting in a resistance order of Col > VP16 ≈ Vbl > Adr. Login to comment 136 ABCB1 p.His61Arg ABCB1 p.His61Lys The ability to confer resistance to Adr of mutant P-glycoproteins showed a characteristic dependence on the nature of the amino acids: although cells expressing mutants in which His61 was replaced by amino acids with side chains larger than His showed higher (more than 2-fold than that of the wild-type) resistance to Adr, cells expressing mutants in which His61 was replaced by Lys or Arg showed markedly lower resistance to Adr. Login to comment