1cdb
STRUCTURE OF THE GLYCOSYLATED ADHESION DOMAIN OF HUMAN T LYMPHOCYTE GLYCOPROTEIN CD2
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OverviewOverview
BACKGROUND: CD2, a T-cell specific surface glycoprotein, is critically, important for mediating adherence of T cells to antigen-presenting cells, or target cells. Domain 1 of human CD2 is responsible for cell adhesion, binding to CD58 (LFA-3) expressed on the cell to which the T cell binds., Human CD2 domain 1 requires N-linked carbohydrate to maintain its native, conformation and ability to bind CD58. In contrast, rat CD2 does not, require N-linked carbohydrate, and binds to a different ligand, CD48., RESULTS: The three-dimensional structure of the glycosylated form of, domain 1 of human CD2 has been determined by NMR spectroscopy. The overall, structure resembles the typical beta-barrel of an immunoglobulin variable, domain. Nuclear Overhauser enhancement contacts between the protein and, the N-linked glycan have been tentatively identified. CONCLUSION: Based on, our results, we propose a model showing how the N-linked glycan might be, positioned in the human CD2 domain 1 structure. The model provides an, explanation for the observed instability of deglycosylated human CD2, and, allows residues that are important for CD58 binding to be differentiated, from those affecting conformational stability via interactions with the, glycan.
About this StructureAbout this Structure
1CDB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2., Withka JM, Wyss DF, Wagner G, Arulanandam AR, Reinherz EL, Recny MA, Structure. 1993 Sep 15;1(1):69-81. PMID:7915183
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