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Journal article

Crystal structure of the complex between human CD8alpha(alpha) and HLA-A2.

Abstract:

The dimeric cell-surface glycoprotein CD8 is crucial to the positive selection of cytotoxic T cells in the thymus. The homodimer CD8alpha(alpha) or the heterodimer alpha beta stabilizes the interaction of the T-cell antigen receptor (TCR) with major histocompatibility complex (MHC) class I/peptide by binding to the class I molecule. Here we report the crystal structure at 2.7 A resolution of a complex between CD8alpha(alpha) and the human MHC molecule HLA-A2, which is associated with peptide....

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Publication status:
Published

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Publisher copy:
10.1038/42523

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
NDM Experimental Medicine
Role:
Author
Journal:
Nature More from this journal
Volume:
387
Issue:
6633
Pages:
630-634
Publication date:
1997-06-01
DOI:
EISSN:
1476-4687
ISSN:
0028-0836
Language:
English
Keywords:
Pubs id:
pubs:11483
UUID:
uuid:f7f37f0a-4c78-4e71-8319-1df1f00cb1ee
Local pid:
pubs:11483
Source identifiers:
11483
Deposit date:
2012-12-19

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