PMID: 9872322

Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH
Crystal structure of the ATP-binding subunit of an ABC transporter.
Nature. 1998 Dec 17;396(6712):703-7., 1998-12-17 [PubMed]
Sentences
No. Mutations Sentence Comment
185 ABCB2 p.Gly44Ser
X
ABCB2 p.Gly44Ser 9872322:185:46
status: NEW
view ABCB2 p.Gly44Ser details
 Proteins with the mutations G39D, G39R, G39K, G44S, K45P, K45V or K45N are defective in nucleotide binding, ATP hydrolysis and ligand translocation. Login to comment 187 ABCB3 p.Asp178Lys
X
ABCB3 p.Asp178Lys 9872322:187:80
status: NEW
view ABCB3 p.Asp178Lys details
ABCB3 p.Asp178Arg
X
ABCB3 p.Asp178Arg 9872322:187:70
status: NEW
view ABCB3 p.Asp178Arg details
 As would be expected from the crystal structure, mutation of Asp 178 (D178R and D178K) results in defective nucleotide binding and transport. Login to comment 224 ABCC7 p.Leu90Ser
X
ABCC7 p.Leu90Ser 9872322:224:107
status: NEW
view ABCC7 p.Leu90Ser details
 All of the residues involved are located in arm II (Fig. 4) and can be divided into three groups: group 1, L90S, P172T/L and T205A/M are located on the surface on one side of arm II; group 2, E187K, E191K and E212K/G are on the surface on the other side; and group 3, V98A, M206I, V192M and T96(+T) are buried. Login to comment