Definition of peptide binding motifs amongst the HLA-A*30 allelic group.

HLA class I molecules present endogenously processed peptide ligands for surveillance by the T-cell receptor. This potentially immunogenic surface of HLA and peptide is a consequence of the polymorphism found within the HLA molecule and its preference for ligand binding together with peptide conform...

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Main Authors: Krausa, P, Münz, C, Keilholz, W, Stevanovic, S, Jones, E, Browning, M, Bunce, M, Rammensee, H, McMichael, A
Format: Journal article
Language:English
Published: 2000
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author Krausa, P
Münz, C
Keilholz, W
Stevanovic, S
Jones, E
Browning, M
Bunce, M
Rammensee, H
McMichael, A
author_facet Krausa, P
Münz, C
Keilholz, W
Stevanovic, S
Jones, E
Browning, M
Bunce, M
Rammensee, H
McMichael, A
author_sort Krausa, P
collection OXFORD
description HLA class I molecules present endogenously processed peptide ligands for surveillance by the T-cell receptor. This potentially immunogenic surface of HLA and peptide is a consequence of the polymorphism found within the HLA molecule and its preference for ligand binding together with peptide conformation within the binding groove. To investigate the relation between the polymorphic differences between some closely related HLA alleles and their effect on peptide preference, transfectants were established, each containing one of four allelic variants of HLA-A*30. Peptides from all four transfectants were eluted, and both individual ligands and peptide pools were sequenced. The data shows two distinct peptide motifs which distinguish A*3001 from the other three known A*30 variants. Differences in preferences at minor positions within the peptide sequence were noted between A*3002, A*3003 and A*3004, providing additional evidence of the implications of sequence polymorphism to HLA function.
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spelling oxford-uuid:46e92f71-e5d3-4692-bd96-406f2430a54d2022-03-26T15:16:44ZDefinition of peptide binding motifs amongst the HLA-A*30 allelic group.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:46e92f71-e5d3-4692-bd96-406f2430a54dEnglishSymplectic Elements at Oxford2000Krausa, PMünz, CKeilholz, WStevanovic, SJones, EBrowning, MBunce, MRammensee, HMcMichael, AHLA class I molecules present endogenously processed peptide ligands for surveillance by the T-cell receptor. This potentially immunogenic surface of HLA and peptide is a consequence of the polymorphism found within the HLA molecule and its preference for ligand binding together with peptide conformation within the binding groove. To investigate the relation between the polymorphic differences between some closely related HLA alleles and their effect on peptide preference, transfectants were established, each containing one of four allelic variants of HLA-A*30. Peptides from all four transfectants were eluted, and both individual ligands and peptide pools were sequenced. The data shows two distinct peptide motifs which distinguish A*3001 from the other three known A*30 variants. Differences in preferences at minor positions within the peptide sequence were noted between A*3002, A*3003 and A*3004, providing additional evidence of the implications of sequence polymorphism to HLA function.
spellingShingle Krausa, P
Münz, C
Keilholz, W
Stevanovic, S
Jones, E
Browning, M
Bunce, M
Rammensee, H
McMichael, A
Definition of peptide binding motifs amongst the HLA-A*30 allelic group.
title Definition of peptide binding motifs amongst the HLA-A*30 allelic group.
title_full Definition of peptide binding motifs amongst the HLA-A*30 allelic group.
title_fullStr Definition of peptide binding motifs amongst the HLA-A*30 allelic group.
title_full_unstemmed Definition of peptide binding motifs amongst the HLA-A*30 allelic group.
title_short Definition of peptide binding motifs amongst the HLA-A*30 allelic group.
title_sort definition of peptide binding motifs amongst the hla a 30 allelic group
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