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PDBsum entry 1cdb
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T lymphocyte adhesion glycoprotein
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PDB id
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1cdb
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References listed in PDB file
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Key reference
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Title
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Structure of the glycosylated adhesion domain of human t lymphocyte glycoprotein cd2.
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Authors
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J.M.Withka,
D.F.Wyss,
G.Wagner,
A.R.Arulanandam,
E.L.Reinherz,
M.A.Recny.
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Ref.
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Structure, 1993,
1,
69-81.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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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.
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Secondary reference #1
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Title
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1h resonance assignments and secondary structure of the 13.6 kda glycosylated adhesion domain of human cd2.
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Authors
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D.F.Wyss,
J.M.Withka,
M.H.Knoppers,
K.A.Sterne,
M.A.Recny,
G.Wagner.
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Ref.
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Biochemistry, 1993,
32,
10995-11006.
[DOI no: ]
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PubMed id
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