PMID: 23716676

Shintre CA, Pike AC, Li Q, Kim JI, Barr AJ, Goubin S, Shrestha L, Yang J, Berridge G, Ross J, Stansfeld PJ, Sansom MS, Edwards AM, Bountra C, Marsden BD, von Delft F, Bullock AN, Gileadi O, Burgess-Brown NA, Carpenter EP
Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states.
Proc Natl Acad Sci U S A. 2013 Jun 11;110(24):9710-5. doi: 10.1073/pnas.1217042110. Epub 2013 May 28., [PubMed]
Sentences
No. Mutations Sentence Comment
128 ABCB10 p.Glu659Gln
X
ABCB10 p.Glu659Gln 23716676:128:45
status: NEW
view ABCB10 p.Glu659Gln details
 Mutation of the conserved putative catalytic Glu659 to glutamine in the nucleotide binding site of ABCB10 gave protein with no detectable activity (Fig. S6 B and E), as is observed for other ABC transporters (32, 33). Login to comment 129 ABCB10 p.Arg691His
X
ABCB10 p.Arg691His 23716676:129:89
status: NEW
view ABCB10 p.Arg691His details
 The first construct used for crystallization had a PCR-derived mutation, which converted Arg691 to a histidine. Login to comment 130 ABCB10 p.Arg691His
X
ABCB10 p.Arg691His 23716676:130:4
status: NEW
view ABCB10 p.Arg691His details
 The R691H mutation led to a substantial loss of activity and ATPase activity was restored when the Arg691 was reintroduced (Fig. S6D). Login to comment