ABCB3 p.Cys362Ala
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PMID: 26324772
[PubMed]
Geng J et al: "Use of Functional Polymorphisms To Elucidate the Peptide Binding Site of TAP Complexes."
No.
Sentence
Comment
154
To further investigate which cysteine residue within the internal cavity of the wild-type rTAP becomes conjugated with TC6R, two mutant constructs (rTAP1[C273A] and rTAP2a[C362A]) were generated and tested for cross-linking to the TC6R peptide.
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ABCB3 p.Cys362Ala 26324772:154:172
status: NEW157 In contrast, the rTAP1(C175A)/TAP2a and the rTAP1/TAP2a(C362A) mutants retained the ability to crosslink with the TC6R peptide (Fig. 3D).
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ABCB3 p.Cys362Ala 26324772:157:56
status: NEW213 Top panel, Cross-linking between TC2R or TC6R (1 mM) and wild-type or mutants, rTAP1(C175A)/TAP2a (T1C175A/T2), rTAP1/TAP2a(C362A) (T1/T2C362A), and rTAP1(C273A)/TAP2a (T1C273A/T2).
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ABCB3 p.Cys362Ala 26324772:213:124
status: NEW227 To avoid cross-linking to other cysteine residues in the vicinity of the cavity, the cysteine mutants were generated on the rTAP1(C273A)/TAP2a(C362A) background (named rTAP1*/TAP2a*) to remove the other cysteines that face the internal cavity of the TAP heterodimer (Fig. 3A).
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ABCB3 p.Cys362Ala 26324772:227:143
status: NEW295 All constructs shown in the figure are on the rTAP1(C273A)/TAP2a(C362A) background (labeled as T1*/T2*).
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ABCB3 p.Cys362Ala 26324772:295:65
status: NEW