ABCB2 p.Ser353Cys
Predicted by SNAP2: | A: N (78%), C: N (53%), D: N (57%), E: N (53%), F: D (53%), G: N (57%), H: N (61%), I: N (72%), K: N (72%), L: D (53%), M: N (57%), N: N (97%), P: D (63%), Q: N (66%), R: D (53%), T: N (97%), V: N (53%), W: D (63%), Y: N (53%), |
Predicted by PROVEAN: | A: N, C: D, D: N, E: N, F: D, G: D, H: D, I: D, K: N, L: D, M: D, N: N, P: D, Q: N, R: N, T: N, V: N, W: D, Y: D, |
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[hide] Single residue within the antigen translocation co... Proc Natl Acad Sci U S A. 2010 May 18;107(20):9135-40. Epub 2010 May 3. Baldauf C, Schrodt S, Herget M, Koch J, Tampe R
Single residue within the antigen translocation complex TAP controls the epitope repertoire by stabilizing a receptive conformation.
Proc Natl Acad Sci U S A. 2010 May 18;107(20):9135-40. Epub 2010 May 3., [PMID:20439763]
Abstract [show]
The recognition of virus infected or malignantly transformed cells by cytotoxic T lymphocytes critically depends on the transporter associated with antigen processing (TAP), which delivers proteasomal degradation products into the endoplasmic reticulum lumen for subsequent loading of major histocompatibility complex class I molecules. Here we have identified a single cysteinyl residue in the TAP complex that modulates peptide binding and translocation, thereby restricting the epitope repertoire. Cysteine 213 in human TAP2 was found to be part of a newly uncovered substrate-binding site crucial for peptide recognition. This residue contacts the peptide in the binding pocket in an orientated manner. The translocation complex can be reversibly inactivated by thiol modification of this cysteinyl residue. As part of an unexpected mechanism, this residue is crucial in complementing the binding pocket for a given subset of epitopes as well as in maintaining a substrate-receptive conformation of the translocation complex.
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No. Sentence Comment
47 Surprisingly, CL/CL(S353C), CL/CL(S362C), and CL/CL(V394C) show the same peptide binding and transport activity as the CL/ CL complex (Fig. 1B).
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ABCB2 p.Ser353Cys 20439763:47:20
status: NEW46 Surprisingly, CL/CL(S353C), CL/CL(S362C), and CL/CL(V394C) show the same peptide binding and transport activity as the CL/ CL complex (Fig. 1B).
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ABCB2 p.Ser353Cys 20439763:46:20
status: NEW