ABCMdb

ABCB1 p.Ala129Cys

None has been submitted yet.

Publications

PMID: 14749322 [PubMed] Loo TW et al: "Val133 and Cys137 in transmembrane segment 2 are close to Arg935 and Gly939 in transmembrane segment 11 of human P-glycoprotein."

No. Sentence Comment

124 TABLE I Cross-linking between residues in TM2 and TM11 -, no cross-linked product detected on SDS-polyacrylamide gels at 37 °C; ϩ, relatively weak cross-linking (Ͻ50% of P-gp cross-linked) at 37 °C; ϩϩ, relatively strong cross-linking (Ͼ50% of P-gp cross-linked) at 37 °C; *, cross-linked product also detected at 22 °C; **, cross-linked product also detected at 22 and 4 °C. TM2 TM11 A935C H936C I937C F938C G939C I940C T941C F942C S943C F944C A128C - - - - - - - - - - A129C - - - - - - - - - - Y130C - - - - ϩ ϩ - ϩ ϩ - I131C - - - - - - - - - - Q132C - - - - - - - - - - V133C - - - ϩ ϩϩ, ** - - ϩ ϩ - S134C ϩ ϩ - - ϩ ϩ - - - - F135C - - - - - - - - - - W136C - - - - - - - - - - C137C ϩϩ, ** - - - ϩ - - - - - L138C ϩϩ, * - - - - - - - - - TM11 are close to each other at their cytoplasmic ends. Login to comment

PMID: 15709779 [PubMed] Kaur P et al: "Biochemical characterization of domains in the membrane subunit DrrB that interact with the ABC subunit DrrA: identification of a conserved motif."

No. Sentence Comment

77 The mutants were named S4C, S15C, S23C, S35C, A44C, C260S up: 5'-GGCCTGGTCCTGTCCGTGTCGGCAGGG-3' C260S dn: 5'-CCCTGCCGACACGGACAGGACCAGGCC-3' S23C up: 5'- CGGACGGTGCTGTGCGCGGGTGAACGG-3' S23C dn: 5'- CCGTTCACCCGCGCACAGCACCGTCCG-3' V53C, T70C, S80C, V92C, S107C, V116C, A129C, T149C, A160C, V173C, S213C, S236C, T249C, A270C, and A282C, respectively. Login to comment
168 substitutions, including V53C, T70C, V92C, A129C, S236C, and S249C, showed a decrease in resistance to doxorubicin (Table 1). Login to comment
193 The location of the cross-linked species is marked as A+B. (A) S23C (positive control), A129C, T149C, A160C. Login to comment
196 Table 1: Doxorubicin Resistance of E. coli N43 Cells Expressing Wild Type DrrA with DrrB Containing Different Cysteine Substitutionsa amt of dox, µg/mLdomain of DrrB location of cysteine 0 4 6 8 (wild type) C260 +++ +++ +++ ++ N-terminus S15C +++ +++ +++ ++ N-terminus S23C +++ +++ +++ ++ N-terminus S35C +++ +++ ++ ++ N-terminus A44C +++ +++ ++ + TM 1 V53C +++ ++ ++ - TM 1 T70C +++ + + + P 1 S80C +++ ++ + - TM 2 V92C +++ ( - - TM 2 S107C +++ +++ ++ ++ C 1 V116C +++ +++ +++ ++ TM 3 A129C +++ ++ + - TM 4 T149C +++ ++ ++ + C 2 A160C +++ +++ ++ + TM 5 V173C +++ +++ ++ + TM 6 S213C +++ +++ ++ + C 3 S236C +++ ++ + - TM 7 S249C +++ + + - TM 8 A270C +++ +++ ++ ++ C-terminus A282C +++ +++ ++ ++ cysteine-less DrrB C260S +++ +++ +++ +++ vector only pSU2718 ++++ ( - - a Legend: +++, very good growth; ++, good growth; +, some growth; -, no growth. Login to comment
278 Six (V53C, T70C, V92C, A129C, S236C, S249C) out of 20 substitutions created in this study, however, showed varying levels of doxorubicin-sensitive phenotype (Table 1). Login to comment
281 Secondary structure analysis by the Chou-Fasman method showed that five (V53C, T70C, V92C, A129C, S249C) of these six mutants, which resulted in doxorubicin sensitivity, showed no change at all in their predicted secondary structure, the exception being S236C, which showed a split in the helical stretch predicted between residues 226 and 248 in the C terminus of DrrB. Login to comment