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Cutting edge: HLA-B27 can form a novel beta 2-microglobulin-free heavy chain homodimer structure.

Abstract:

HLA-B27 has a striking association with inflammatory arthritis. We show that free HLA-B27 heavy chains can form a disulfide-bonded homodimer, dependent on residue Cys67 in their extracellular alpha 1 domain. Despite the absence of beta 2-microglobulin, HLA-B27 heavy chain homodimers (termed HC-B27) were stabilized by a known peptide epitope. HC-B27 complexes were recognized by the conformation-specific Ab W6/32, but not the ME1 Ab. Surface labeling and immunoprecipitation demonstrated the pre...

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Publication status:
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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
CCMP
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
NDM Experimental Medicine
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
NDM Experimental Medicine
Role:
Author
Journal:
Journal of Immunology
Volume:
162
Issue:
9
Pages:
5045-5048
Publication date:
1999-05-01
EISSN:
1550-6606
ISSN:
0022-1767
Source identifiers:
14495
Language:
English
Keywords:
Pubs id:
pubs:14495
UUID:
uuid:3ee4d8b1-b669-4523-ab59-fa9780f356bf
Local pid:
pubs:14495
Deposit date:
2012-12-19

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