ABCB3 p.Leu266Phe
| Predicted by SNAP2: | A: N (61%), C: N (57%), D: D (71%), E: D (71%), F: N (57%), G: N (53%), H: N (53%), I: N (66%), K: D (75%), M: N (82%), N: D (63%), P: D (80%), Q: D (66%), R: D (71%), S: D (63%), T: D (59%), V: N (72%), W: D (66%), Y: N (57%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: N, G: D, H: D, I: N, K: D, M: N, N: D, P: D, Q: D, R: D, S: D, T: D, V: N, 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
129 As shown in the peptide transport analysis (Fig. 2A, 2B), rTAP1/TAP2a(Q262R), rTAP1/TAP2a(S265P), and rTAP1/TAP2a (L266F) displayed transport efficiencies quite similar to the wild-type rTAP1/TAP2a complex for both peptides.
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ABCB3 p.Leu266Phe 26324772:129:115
status: NEW133 To address whether other polymorphic rTAP2 residues have synergistic effects, we introduced a combination of four mutations within TM2 and TM3, which resulted in the quadruple mutant construct rTAP1/TAP2a (E218M/Q262R/S265P/L266F).
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ABCB3 p.Leu266Phe 26324772:133:224
status: NEW136 Similar results were obtained for the effects of the single (E218M) and quadruple (E218M/Q262R/S265P/L266F) mutations in rTAP2a upon transport of a pair of decapeptides, RYWANATK*SR (RR) and RYWANATK*SF (RF).
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ABCB3 p.Leu266Phe 26324772:136:101
status: NEW186 The quadruple mutant of rat TAP, TAP1/TAP2a(E218M/Q262R/ S265P/L266F), is indicated as EQSL/MPRF.
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ABCB3 p.Leu266Phe 26324772:186:63
status: NEW245 Binding of indicated TR (A) or TV (B) peptides to wild-type rTAP1/TAP2a (shown as WT), single mutant rTAP1/TAP2a(E218M) and quadruple mutant rTAP1/TAP2a(E218M/Q262R/S265P/L266F) (shown as EQSL/MRPF) was assessed using BMOE-mediated cross-linking assays, performed as described in Fig. 3.
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ABCB3 p.Leu266Phe 26324772:245:171
status: NEW