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PDBsum entry 1url
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Sugar binding protein/immune system
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PDB id
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1url
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References listed in PDB file
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Key reference
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Title
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Complex of sialoadhesin with a glycopeptide ligand.
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Authors
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J.T.Bukrinsky,
P.M.St hilaire,
M.Meldal,
P.R.Crocker,
A.Henriksen.
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Ref.
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Biochim Biophys Acta, 2004,
1702,
173-179.
[DOI no: ]
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PubMed id
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Abstract
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Sialoadhesin is a sialic acid-binding immunoglobulin-like lectin (Siglec),
expressed on subsets of macrophages. It is a model system for Siglec
receptor-mediated cell surface interactions through binding of sialylated
glycoconjugates. The N-terminal sialoadhesin domain can mediate sialic
acid-binding on its own. The structure of this domain has been determined in
complex with a sialic acid-containing heptapeptide,
(Ala-Gly-His-Thr(Neu5Ac)-Trp-Gly-His). The affinity of sialoadhesin for this
ligand is four times higher than the affinity for the natural linkage
2,3'-sialyllactose. The structure of the glycopeptide complex suggests
strategies for ligand optimization and provides possible explanations for the
observed differences in specificities among the Siglecs.
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Secondary reference #1
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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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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
reproduced from the cited reference
with permission from Cell Press
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