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PDBsum entry 1g1r
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Immune system, membrane protein
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PDB id
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1g1r
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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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Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of p- And e-Selectin bound to sle(X) and psgl-1.
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Authors
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W.S.Somers,
J.Tang,
G.D.Shaw,
R.T.Camphausen.
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Ref.
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Cell, 2000,
103,
467-479.
[DOI no: ]
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PubMed id
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Abstract
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P-, E- and L-selectin constitute a family of cell adhesion receptors that
mediate the initial tethering and rolling of leukocytes on inflamed endothelium
as a prelude to their firm attachment and extravasation into tissues. The
selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with
high-affinity to specific glycoprotein counterreceptors, including PSGL-1. Here,
we report crystal structures of human P- and E-selectin constructs containing
the lectin and EGF (LE) domains co-complexed with SLe(X). We also present the
crystal structure of P-selectin LE co-complexed with the N-terminal domain of
human PSGL-1 modified by both tyrosine sulfation and SLe(X). These structures
reveal differences in how E- and P-selectin bind SLe(X) and the molecular basis
of the high-affinity interaction between P-selectin and PSGL-1.
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Figure 1.
Figure 1. Comparison of P-LE to the Structure of E-LE
([17])(A) Ribbon representation of the optimal superposition of
P-LE and the previously described E-LE structure showing overall
similarity. P-LE is in blue and E-LE is in green. The bound
calcium ions in the two structures are precisely superimposed
and are represented as a single yellow sphere.(B) A ball and
stick representation of the superposition of P-LE and E-LE
residues in the vicinity of the SLe^X binding site. The coloring
scheme and superposition of calcium ions is identical to that in
Figure 1A. For clarity, only interactions with the bound calcium
in E-LE are shown as dashed lines. The stabilizing hydrogen bond
between Arg97 and Asp100 in E-selectin is also shown as a dashed
line. For residues that differ between E- and P-selectin,
E-selectin residues are listed first. All structure figures were
produced with MOLSCRIPT ( [20]) and RASTER3D ( [27]) except
where noted.
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Figure 6.
Figure 6. Structure of the P-LE/SGP-3 Complex and Binding
Interactions Involving Tys Residues(A) Ribbon/stick
representation of the P-LE/SGP-3 structure superimposed on the
unliganded structure of P-LE. The unliganded structure of P-LE
is shown in blue, complexed P-LE in purple, and SGP-3 in orange.
The bound strontium ion in the P-LE/SGP-3 complex is directly
superimposed over the calcium ion in unliganded P-LE and is
shown as a green sphere. The MPD molecule that is found at the
lectin-EGF domain interface in the P-LE/SGP-3 complex is shown
in dark blue.(B) Stereo view of a close-up of P-LE/SGP-3
interactions in the region of Tys7 (in orange) illustrating the
hydrogen bonding network with P-LE (purple). The sulfur atom in
Tys7 is shown in yellow.(C) Stereo view of a close-up of the
P-LE/SGP-3 interaction in the region of Tys10 and the Fuc
binding site illustrating the change in conformation and binding
contacts for the Asn83 to Asp89 loop within P-LE. Uncomplexed
P-LE is shown in blue and P-LE complexed with SGP-3 is shown in
purple. SGP-3 residues are shown in orange (the sulfur atom of
Tys10 is in yellow) and the bound strontium ion is shown as a
green sphere. The portion of SGP-3 omitted for clarity is shown
as an orange ellipse.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2000,
103,
467-479)
copyright 2000.
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