PMID: 9636053

Beaudet L, Urbatsch IL, Gros P
Mutations in the nucleotide-binding sites of P-glycoprotein that affect substrate specificity modulate substrate-induced adenosine triphosphatase activity.
Biochemistry. 1998 Jun 23;37(25):9073-82., 1998-06-23 [PubMed]
Sentences
No. Mutations Sentence Comment
243 ABCB1 p.Gly185Val
X
ABCB1 p.Gly185Val 9636053:243:74
status: NEW
view ABCB1 p.Gly185Val details
It is interesting to note that the altered drug resistance profile of the G185V mutation in the human MDR1 (23, 55) has also been found associated with alterations in the pattern of drug-stimulatable ATPase activity (56, 57). Login to comment
246 ABCB1 p.Lys536Arg
X
ABCB1 p.Lys536Arg 9636053:246:110
status: NEW
view ABCB1 p.Lys536Arg details
Another NBD mutation known to affect substrate specificity is the enhanced colchicine resistance noted in the K536R variant of human MDR1 (45). Login to comment
247 ABCB1 p.Lys536Arg
X
ABCB1 p.Lys536Arg 9636053:247:12
status: NEW
view ABCB1 p.Lys536Arg details
Remarkably, K536R maps within the highly conserved dodecapeptide segment immediately upstream from the Walker B motif and immediately downstream from the ERGA/DKGT substitution studied in this report. Login to comment
248 ABCB1 p.Lys536Arg
X
ABCB1 p.Lys536Arg 9636053:248:68
status: NEW
view ABCB1 p.Lys536Arg details
The biochemical basis of the altered drug resistance profile in the K536R mutation has not yet been clarified, although it did not seem to affect binding of the photoactive probe [125I]iodomycin (45). Login to comment