ABCB3 p.Glu602Cys
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PMID: 19297616
[PubMed]
Oancea G et al: "Structural arrangement of the transmission interface in the antigen ABC transport complex TAP."
No.
Sentence
Comment
57
Remarkably, the X-loop mutations showed a reduced transport activity, with 50% transport activity for E602C and 20% for E602D or E602A (Fig. 2B).
X
ABCB3 p.Glu602Cys 19297616:57:102
status: NEW58 Complete disruption of peptide transport was observed for the E602R mutant.
X
ABCB3 p.Glu602Cys 19297616:58:102
status: NEW63 Altogether, 24 single-cysteine TAP1 mutants were coexpressed with TAP2(E602C) and yielded similar expression levels (Fig. 3A).
X
ABCB3 p.Glu602Cys 19297616:63:71
status: NEW89 TAP cross-linking conditions using copper phenanthroline (CuPhe) were established for the A381/E602C complex (Fig. 4A and Fig. S2).
X
ABCB3 p.Glu602Cys 19297616:89:95
status: NEW100 These findings demonstrate the specificity of the cross-linking between the X-loop (E602C) of TAP2 and CL1/2 of TAP1.
X
ABCB3 p.Glu602Cys 19297616:100:84
status: NEW121 Specific peptide binding and transport of TAP1(Cys-less)/TAP2(E602C) was normalized to 100%.
X
ABCB3 p.Glu602Cys 19297616:121:62
status: NEW129 We chose 2 pairs of mutations, Q277C/E602C and A381C/E602C, containing a single cysteine in each coupling helix of TAP1.
X
ABCB3 p.Glu602Cys 19297616:129:37
status: NEWX
ABCB3 p.Glu602Cys 19297616:129:53
status: NEW131 Strikingly, cross-linking of the A381C/E602C complex impeded both peptide binding and transport, in contrast to the combination with Cys-less TAP1 (Fig. 5B).
X
ABCB3 p.Glu602Cys 19297616:131:39
status: NEW132 Surprisingly, cross-linking of Q277C/E602C arrested TAP in a translocation-incompetent state, in which peptide binding was unaffected (Fig. 5C).
X
ABCB3 p.Glu602Cys 19297616:132:37
status: NEWX
ABCB3 p.Glu602Cys 19297616:132:39
status: NEW133 The transport activity of Cys-less/E602C is only slightly reduced due to irreversible oxidation.
X
ABCB3 p.Glu602Cys 19297616:133:35
status: NEW161 (B and C) The cross-linking of the single-cysteine mutants of CL1 (B) and CL2 (C) in TAP1 with E602C of TAP2.
X
ABCB3 p.Glu602Cys 19297616:161:95
status: NEW201 Membranes (500 g of protein) containing variants of TAP1 in combination with TAP2(E602C) were incubated in the presence or absence of CuPhe for 1 min at 4 °C.
X
ABCB3 p.Glu602Cys 19297616:201:90
status: NEW64 Altogether, 24 single-cysteine TAP1 mutants were coexpressed with TAP2(E602C) and yielded similar expression levels (Fig. 3A).
X
ABCB3 p.Glu602Cys 19297616:64:71
status: NEW90 TAP cross-linking conditions using copper phenanthroline (CuPhe) were established for the A381/E602C complex (Fig. 4A and Fig. S2).
X
ABCB3 p.Glu602Cys 19297616:90:95
status: NEW101 These findings demonstrate the specificity of the cross-linking between the X-loop (E602C) of TAP2 and CL1/2 of TAP1.
X
ABCB3 p.Glu602Cys 19297616:101:84
status: NEW122 Specific peptide binding and transport of TAP1(Cys-less)/TAP2(E602C) was normalized to 100%.
X
ABCB3 p.Glu602Cys 19297616:122:62
status: NEW130 We chose 2 pairs of mutations, Q277C/E602C and A381C/E602C, containing a single cysteine in each coupling helix of TAP1.
X
ABCB3 p.Glu602Cys 19297616:130:37
status: NEWX
ABCB3 p.Glu602Cys 19297616:130:53
status: NEW134 The transport activity of Cys-less/E602C is only slightly reduced due to irreversible oxidation.
X
ABCB3 p.Glu602Cys 19297616:134:35
status: NEW163 (B and C) The cross-linking of the single-cysteine mutants of CL1 (B) and CL2 (C) in TAP1 with E602C of TAP2.
X
ABCB3 p.Glu602Cys 19297616:163:95
status: NEW203 Membranes (500 òe;g of protein) containing variants of TAP1 in combination with TAP2(E602C) were incubated in the presence or absence of CuPhe for 1 min at 4 &#b0;C.
X
ABCB3 p.Glu602Cys 19297616:203:89
status: NEW91 TAP cross-linking conditions using copper phenanthroline (CuPhe) were established for the A381/E602C complex (Fig. 4A and Fig. S2).
X
ABCB3 p.Glu602Cys 19297616:91:95
status: NEW102 These findings demonstrate the specificity of the cross-linking between the X-loop (E602C) of TAP2 and CL1/2 of TAP1.
X
ABCB3 p.Glu602Cys 19297616:102:84
status: NEW124 Specific peptide binding and transport of TAP1(Cys-less)/TAP2(E602C) was normalized to 100%.
X
ABCB3 p.Glu602Cys 19297616:124:62
status: NEW135 Surprisingly, cross-linking of Q277C/E602C arrested TAP in a translocation-incompetent state, in which peptide binding was unaffected (Fig. 5C).
X
ABCB3 p.Glu602Cys 19297616:135:37
status: NEW136 The transport activity of Cys-less/E602C is only slightly reduced due to irreversible oxidation.
X
ABCB3 p.Glu602Cys 19297616:136:35
status: NEW165 (B and C) The cross-linking of the single-cysteine mutants of CL1 (B) and CL2 (C) in TAP1 with E602C of TAP2.
X
ABCB3 p.Glu602Cys 19297616:165:95
status: NEW205 Membranes (500 òe;g of protein) containing variants of TAP1 in combination with TAP2(E602C) were incubated in the presence or absence of CuPhe for 1 min at 4 &#b0;C.
X
ABCB3 p.Glu602Cys 19297616:205:89
status: NEW