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PDBsum entry 1hng
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T lymphocyte adhesion glycoprotein
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PDB id
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1hng
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure at 2.8 a resolution of a soluble form of the cell adhesion molecule cd2.
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Authors
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E.Y.Jones,
S.J.Davis,
A.F.Williams,
K.Harlos,
D.I.Stuart.
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Ref.
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Nature, 1992,
360,
232-239.
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PubMed id
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Abstract
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The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides
the first complete view of the extracellular region of a cell adhesion molecule.
The topology of the molecule, which comprises two immunoglobulin-like domains,
is the same as that of the first two domains of CD4 but the relative domain
orientation is altered by a fairly flexible linker region. The putative
ligand-binding beta-sheet forms a flat surface towards the top of the molecule.
Crystal contacts between these surfaces suggest a plausible model for the
adhesive interaction.
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Secondary reference #1
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Title
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Ligand binding by the immunoglobulin superfamily recognition molecule cd2 is glycosylation-Independent.
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Authors
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S.J.Davis,
E.A.Davies,
A.N.Barclay,
S.Daenke,
D.L.Bodian,
E.Y.Jones,
D.I.Stuart,
T.D.Butters,
R.A.Dwek,
P.A.Van der merwe.
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Ref.
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J Biol Chem, 1995,
270,
369-375.
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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
percentage match of
91%.
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Secondary reference #2
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Title
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Expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the t-Cell glycoprotein cd2.
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Authors
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S.J.Davis,
M.J.Puklavec,
D.A.Ashford,
K.Harlos,
E.Y.Jones,
D.I.Stuart,
A.F.Williams.
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Ref.
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Protein Eng, 1993,
6,
229-232.
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PubMed id
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