ABCMdb

PMID: 10204114

Aguilar-Bryan L, Bryan J
Molecular biology of adenosine triphosphate-sensitive potassium channels.
Endocr Rev. 1999 Apr;20(2):101-35., [PubMed]

Sentences

No. Mutations Sentence Comment

277 ABCC8 p.Asn10Gln The N10Q or N1050Q mutations partially eliminate glycosylation, while the double mutant is not glycosylated. Login to comment 526 ABCC8 p.Lys719Arg For example, the K719R mutation in the conserved Walker A motif that is involved in binding of the ␣- and beta-phosphates has no effect on the ATP sensitivity of reconstituted channels (190), although Ueda et al. (239) show that SUR1K719R does not photolabel with [32 P] 8-azido ATP. Login to comment 704 ABCC8 p.Leu3Pro Thomas et al. (284) reported on a KIR6.2 mutation, a leu3pro change, L147P, near the external side of M2, which demonstrated that mutations in the inward rectifier led to PHHI. Login to comment 740 ABCC8 p.Gly716Val Two of these mutations are expected to lead to severe truncations of SUR1 in or near NBF1, while the third mutation results in a gly3val substitution at position 716, G716V, in the Walker A motif. Login to comment 754 ABCC8 p.Gly716Val With the exception of the severe truncations and the G716V mutation, the SUR1 mutants retain high-affinity sulfonylurea binding activity, suggesting their folding is not completely aberrant. Login to comment