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* Residue conservation analysis
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DOI no:
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Mol Cell
1:719-728
(1998)
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PubMed id:
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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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A.P.May,
R.C.Robinson,
M.Vinson,
P.R.Crocker,
E.Y.Jones.
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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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Selected figure(s)
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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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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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PDB codes:
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P.Kursula
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Amino Acids,
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Y.Liu,
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PDB codes:
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E.Koh,
T.Kim,
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Bioinformatics,
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B.S.Bochner,
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C.Burlak,
L.M.Twining,
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Transplantation,
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C.P.Swaminathan,
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Chembiochem,
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Sialic acid recognition by Vibrio cholerae neuraminidase.
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J Biol Chem,
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PDB codes:
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N.Dimasi,
A.Moretta,
L.Moretta,
R.Biassoni,
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Structure of the saccharide-binding domain of the human natural killer cell inhibitory receptor p75/AIRM1.
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Acta Crystallogr D Biol Crystallogr,
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PDB code:
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P.L.Delputte,
and
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(2004).
Porcine arterivirus infection of alveolar macrophages is mediated by sialic acid on the virus.
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J Virol,
78,
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Large-scale sequencing of the CD33-related Siglec gene cluster in five mammalian species reveals rapid evolution by multiple mechanisms.
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Negative regulation of T cell receptor signaling by Siglec-7 (p70/AIRM) and Siglec-9.
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J Biol Chem,
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C.Linington,
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Structural insights into the antigenicity of myelin oligodendrocyte glycoprotein.
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Proc Natl Acad Sci U S A,
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PDB codes:
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C.Jones,
M.Virji,
and
P.R.Crocker
(2003).
Recognition of sialylated meningococcal lipopolysaccharide by siglecs expressed on myeloid cells leads to enhanced bacterial uptake.
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Mol Microbiol,
49,
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C.S.Clements,
H.H.Reid,
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The crystal structure of myelin oligodendrocyte glycoprotein, a key autoantigen in multiple sclerosis.
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Proc Natl Acad Sci U S A,
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PDB code:
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L.Buts,
J.Bouckaert,
E.De Genst,
R.Loris,
S.Oscarson,
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E.Brosens,
L.Wyns,
and
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The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine.
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Mol Microbiol,
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PDB codes:
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M.S.Alphey,
H.Attrill,
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High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec family.
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J Biol Chem,
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N.R.Zaccai,
K.Maenaka,
T.Maenaka,
P.R.Crocker,
R.Brossmer,
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Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin.
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Structure,
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N.Vanderheijden,
P.L.Delputte,
H.W.Favoreel,
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Involvement of sialoadhesin in entry of porcine reproductive and respiratory syndrome virus into porcine alveolar macrophages.
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Sialoside specificity of the siglec family assessed using novel multivalent probes: identification of potent inhibitors of myelin-associated glycoprotein.
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J Biol Chem,
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The ligand-binding domain of CD22 is needed for inhibition of the B cell receptor signal, as demonstrated by a novel human CD22-specific inhibitor compound.
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Cloning and characterization of human Siglec-11. A recently evolved signaling that can interact with SHP-1 and SHP-2 and is expressed by tissue macrophages, including brain microglia.
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J Biol Chem,
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Identification and characterization of a novel siglec, siglec-7, expressed by human natural killer cells and monocytes.
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The myeloid-specific sialic acid-binding receptor, CD33, associates with the protein-tyrosine phosphatases, SHP-1 and SHP-2.
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| |
J Biol Chem,
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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only a partial list as not all journals are covered by
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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