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Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-A resolution.

Abstract:

The binding of the cell surface molecule CD58 (formerly lymphocyte function-associated antigen 3) to its ligand, CD2, significantly increases the sensitivity of antigen recognition by T cells. This was the first heterophilic cell adhesion interaction to be discovered and is now an important paradigm for analyzing the structural basis of cell-cell recognition. The crystal structure of a CD2-binding chimeric form of CD58, solved to 1.8-A resolution, reveals that the ligand binding domain of CD5...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.96.8.4289

Authors


Ikemizu, S More by this author
Sparks, LM More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
96
Issue:
8
Pages:
4289-4294
Publication date:
1999-04-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:0ce15342-a9a2-4340-b1ca-f5cfe7eb7a17
Source identifiers:
30690
Local pid:
pubs:30690

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