PMID: 9640644

Schneider E, Hunke S
ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains.
FEMS Microbiol Rev. 1998 Apr;22(1):1-20., [PubMed]
Sentences
No. Mutations Sentence Comment
1529 ABCB2 p.Val117Met
X
ABCB2 p.Val117Met 9640644:1529:144
status: NEW
view ABCB2 p.Val117Met details
 Suppressor mutations in malK that restored transport of these mutants were found to map mainly in the helical domain of the MalK protein (A85M, V117M) [89], close to those residues which when mutated allowed LacK to substitute more e&#a4;ciently for MalK in maltose transport [92]. Login to comment 1530 ABCB4 p.Val599Ile
X
ABCB4 p.Val599Ile 9640644:1530:71
status: NEW
view ABCB4 p.Val599Ile details
 By using a similar approach, a mutation in the helical domain of HlyB (V599I) was isolated that FEMSRE 605 29-5-98 compensated for a deletion in the substrate molecule HlyA. Login to comment