ABCC8 p.Ala284Lys
| Predicted by SNAP2: | C: N (61%), D: N (82%), E: N (93%), F: D (59%), G: N (87%), H: N (87%), I: N (87%), K: N (93%), L: N (82%), M: N (93%), N: N (87%), P: N (82%), Q: N (93%), R: N (87%), S: N (93%), T: N (93%), V: N (87%), W: D (53%), Y: D (53%), |
| Predicted by PROVEAN: | C: N, D: N, E: N, F: N, G: N, H: N, I: N, K: N, L: N, M: N, N: N, P: N, Q: N, R: N, S: N, T: N, V: N, W: D, Y: N, |
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[hide] HLA-DP4, the most frequent HLA II molecule, define... J Immunol. 2002 Dec 15;169(12):6928-34. Castelli FA, Buhot C, Sanson A, Zarour H, Pouvelle-Moratille S, Nonn C, Gahery-Segard H, Guillet JG, Menez A, Georges B, Maillere B
HLA-DP4, the most frequent HLA II molecule, defines a new supertype of peptide-binding specificity.
J Immunol. 2002 Dec 15;169(12):6928-34., [PMID:12471126]
Abstract [show]
Among HLA-DP specificities, HLA-DP4 specificity involves at least two molecules, HLA-DPA1*0103/DPB1*0401 (DP401) and HLA-DPA1*0103/DPB1*0402 (DP402), which differ from each other by only three residues. Together, they are present worldwide at an allelic frequency of 20-60% and are the most abundant human HLA II alleles. Strikingly, the peptide-binding specificities of these molecules have never been investigated. Hence, in this study, we report the peptide-binding motifs of both molecules. We first set up a binding assay specific for the immunopurified HLA-DP4 molecules. Using multiple sets of synthetic peptides, we successfully defined the amino acid preferences of the anchor residues. With these assays, we were also able to identify new peptide ligands from allergens and viral and tumor Ags. DP401 and DP402 exhibit very similar patterns of recognition in agreement with molecular modeling of the complexes. Pockets P1 and P6 accommodate the main anchor residues and interestingly contain only two polymorphic residues, beta86 and beta11, respectively. Both positions are almost dimorphic and thus produce a limited number of pocket combinations. Taken together, our results support the existence of three main binding supertypes among HLA-DP molecules and should significantly contribute to the identification of universal epitopes to be used in peptide-based vaccines for cancer, as well as for allergic or infectious diseases.
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No. Sentence Comment
122 Alanine and lysine scanning of the Oxy273-285 peptide on DP401 and DP402 moleculesa Peptides Oxy273-285 Sequences KYFAATQFEPLAA 1 4 6 9 DP401 1 (Ϯ0) DP402 1 (Ϯ0) Oxy K273A AYFAATQFEPLAA 1 (Ϯ0.7) 1 (Ϯ0.3) Oxy Y274A KAFAATQFEPLAA 2 (Ϯ0.2) 2 (Ϯ0.5) Oxy F275A KYAAATQFEPLAA 40 (Ϯ25) 7 (Ϯ2.1) Oxy T278A KYFAAAQFEPLAA 1 (Ϯ0.2) 1 (Ϯ0.1) Oxy Q279A KYFAATAFEPLAA 1 (Ϯ0.7) 1 (Ϯ0.3) Oxy F280A KYFAATQAEPLAA 240 (Ϯ100) 75 (Ϯ31) Oxy E281A KYFAATQFAPLAA 0.5 (Ϯ0.3) 0.5 (Ϯ0) Oxy P282A KYFAATQFEALAA 2 (Ϯ0.2) 1 (Ϯ0.1) Oxy L283A KYFAATQFEPAAA 4 (Ϯ1.3) 4 (Ϯ1.3) Oxy Y274K KKFAATQFEPLAA 2 (Ϯ0.2) 3 (Ϯ0.1) Oxy F275K KYKAATQFEPLAA 400 (Ϯ270) 190 (Ϯ160) Oxy A276K KYFKATQFEPLAA 2 (Ϯ0.7) 2 (Ϯ0.2) Oxy A277K KYFAKTQFEPLAA 3 (Ϯ0.9) 2 (Ϯ0.5) Oxy T278K KYFAAKQFEPLAA 30 (Ϯ17) 5 (Ϯ0.4) Oxy Q279K KYFAATKFEPLAA 2 (Ϯ0.1) 1 (Ϯ0.1) Oxy F280K KYFAATQKEPLAA 270 (Ϯ180) 190 (Ϯ135) Oxy E281K KYFAATQFKPLAA 2 (Ϯ0.5) 1 (Ϯ0.2) Oxy P282K KYFAATQFEKLAA 2 (Ϯ1.2) 2 (Ϯ1.5) Oxy L283K KYFAATQFEPKAA 70 (Ϯ45) 80 (Ϯ37) Oxy A284K KYFAATQFEPLKA 2 (Ϯ0.9) 2 (Ϯ0.5) Oxy A285K KYFAATQFEPLAK 2 (Ϯ0.9) 2 (Ϯ0.7) a Capacity of the substituted peptides to bind HLA-DP401 and HLA-DP402 was investigated. Results are presented as relative activity (ratio between native and substituted peptide IC50).
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ABCC8 p.Ala284Lys 12471126:122:1216
status: NEW