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PDBsum entry 1qfo
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Immune system
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PDB id
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1qfo
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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 of the n-Terminal domain of sialoadhesin in complex with 3' Sialyllactose at 1.85 a resolution.
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Authors
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A.P.May,
R.C.Robinson,
M.Vinson,
P.R.Crocker,
E.Y.Jones.
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Ref.
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Mol Cell, 1998,
1,
719-728.
[DOI no: ]
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PubMed id
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Abstract
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The structure of the functional N-terminal domain from the extracellular region
of the cell surface receptor sialoadhesin has been determined in complex with
the oligosaccharide 3' sialyllactose. This provides structural information for
the siglec family of proteins. The structure conforms to the V-set
immunoglobulin-like fold but contains several distinctive features, including an
intra-beta sheet disulphide and a splitting of the standard beta strand G into
two shorter strands. These novel features appear important in adapting the V-set
fold for sialic acid-mediated recognition. Analysis of the complex with
3'sialyllactose highlights three residues, conserved throughout the siglec
family, as key features of the sialic acid-binding template. The complex is
representative of the functional recognition interaction with carbohydrate and
as such provides detailed information for a heterotypic cell adhesion
interaction.
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Figure 2.
Figure 2. The Structure of the N-Terminal Domain of
Sialoadhesin in Complex with 3′ SialyllactoseEach strand is
labeled. The 3′ sialyllactose lies along strand G and makes
interactions with residues from the A,G, and F strands.
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Figure 3.
Figure 3. Superposition of the V-Set Domain from P0 with
SnD1The Cα trace of SnD1 is shown in green; the Cα trace of P0
is shown in yellow.
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(1998,
1,
719-728)
copyright 1998.
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