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Journal article

Naturally processed peptides from two disease-resistance-associated HLA-DR13 alleles show related sequence motifs and the effects of the dimorphism at position 86 of the HLA-DR beta chain.

Abstract:

HLA-DR13 has been associated with resistance to two major infectious diseases of humans. To investigate the peptide binding specificity of two HLA-DR13 molecules and the effects of the Gly/Val dimorphism at position 86 of the HLA-DR beta chain on natural peptide ligands, these peptides were acid-eluted from immunoaffinity-purified HLA-DRB1*1301 and -DRB1*1302, molecules that differ only at this position. The eluted peptides were subjected to pool sequencing or individual peptide sequencing by...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.92.14.6567

Authors


Davenport, MP More by this author
Willis, AC More by this author
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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
92
Issue:
14
Pages:
6567-6571
Publication date:
1995-07-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:07cec052-3d9e-4e6f-91ef-12068d6a021c
Source identifiers:
35638
Local pid:
pubs:35638

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