ABCB3 p.Ser251Cys
| Predicted by SNAP2: | A: D (63%), C: D (71%), D: D (80%), E: D (80%), F: D (80%), G: D (53%), H: D (80%), I: D (80%), K: D (85%), L: D (80%), M: D (66%), N: D (59%), P: D (85%), Q: D (75%), R: D (80%), T: N (72%), V: D (75%), W: D (85%), Y: D (80%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, P: D, Q: D, R: D, T: D, V: D, W: D, Y: D, |
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[hide] Use of Functional Polymorphisms To Elucidate the P... J Immunol. 2015 Oct 1;195(7):3436-48. doi: 10.4049/jimmunol.1500985. Epub 2015 Aug 31. Geng J, Pogozheva ID, Mosberg HI, Raghavan M
Use of Functional Polymorphisms To Elucidate the Peptide Binding Site of TAP Complexes.
J Immunol. 2015 Oct 1;195(7):3436-48. doi: 10.4049/jimmunol.1500985. Epub 2015 Aug 31., [PMID:26324772]
Abstract [show]
TAP1/TAP2 complexes translocate peptides from the cytosol to the endoplasmic reticulum lumen to enable immune surveillance by CD8(+) T cells. Peptide transport is preceded by peptide binding to a cytosol-accessible surface of TAP1/TAP2 complexes, but the location of the TAP peptide-binding pocket remains unknown. Guided by the known contributions of polymorphic TAP variants to peptide selection, we combined homology modeling of TAP with experimental measurements to identify several TAP residues that interact with peptides. Models for peptide-TAP complexes were generated, which indicate bent conformation for peptides. The peptide binding site of TAP is located at the hydrophobic boundary of the cytosolic membrane leaflet, with striking parallels to the glutathione binding site of NaAtm1, a transporter that functions in bacterial heavy metal detoxification. These studies illustrate the conservation of the ligand recognition modes of bacterial and mammalians transporters involved in peptide-guided cellular surveillance.
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No. Sentence Comment
228 We found that the TC2R peptide could be conjugated via BMOE only to rTAP1*(E436C)/TAP2a* but not to rTAP1*(S263C)/ TAP2a* or rTAP1*/TAP2a* (S251C) (Fig. 6B).
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ABCB3 p.Ser251Cys 26324772:228:140
status: NEW232 In contrast, the lack of cross-linking of rTAP1*/TAP2a* (S251C) or rTAP1*(S263C)/TAP2a* mutants to TC2R could not be explained by the impaired binding of these mutants because transport and binding of the TR peptide by rTAP1/TAP2(S251A) and rTAP1(S263A)/TAP2 complexes were not reduced relative to the wild-type TAP (Supplemental Fig. 2).
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ABCB3 p.Ser251Cys 26324772:232:57
status: NEW