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PDBsum entry 4e52
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Sugar binding protein
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PDB id
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4e52
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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 a complex of surfactant protein d (sp-D) and haemophilus influenzae lipopolysaccharide reveals shielding of core structures in sp-D-Resistant strains.
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Authors
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H.W.Clark,
R.M.Mackay,
M.E.Deadman,
D.W.Hood,
J.Madsen,
E.R.Moxon,
J.P.Townsend,
K.B.Reid,
A.Ahmed,
A.J.Shaw,
T.J.Greenhough,
A.K.Shrive.
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Ref.
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Infect Immun, 2016,
84,
1585-1592.
[DOI no: ]
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PubMed id
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Abstract
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The carbohydrate recognition domains (CRDs) of lung collectin surfactant protein
D (SP-D) recognize sugar patterns on the surface of lung pathogens and promote
phagocytosis. Using Haemophilus influenzae Eagan strains expressing
well-characterized lipopolysaccharide (LPS) surface structures of various levels
of complexity, we show that bacterial recognition and binding by SP-D is
inversely related to LPS chain extent and complexity. The crystal structure of a
biologically active recombinant trimeric SP-D CRD complexed with a delipidated
Eagan 4A LPS suggests that efficient LPS recognition by SP-D requires multiple
binding interactions utilizing the three major ligand-binding determinants in
the SP-D binding pocket, with Ca-dependent binding of inner-core heptose
accompanied by interaction of anhydro-Kdo
(4,7-anhydro-3-deoxy-d-manno-oct-2-ulosonic acid) with Arg343 and Asp325.
Combined with enzyme-linked immunosorbent assays (ELISAs) and
fluorescence-activated cell sorter (FACS) binding analyses, our results show
that extended LPS structures previously thought to be targets for collectins are
important in shielding the more vulnerable sites in the LPS core, revealing a
mechanism by which pathogens with complex LPS extensions efficiently evade a
first-line mucosal innate immune defense. The structure also reveals for the
first time the dominant form of anhydro-Kdo.
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Secondary reference #1
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Title
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Structural characterisation of ligand-Binding determinants in human lung surfactant protein d: influence of asp325.
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Authors
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A.K.Shrive,
C.Martin,
I.Burns,
J.M.Paterson,
J.D.Martin,
J.P.Townsend,
P.Waters,
H.W.Clark,
U.Kishore,
K.B.Reid,
T.J.Greenhough.
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Ref.
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J Mol Biol, 2009,
394,
776-788.
[DOI no: ]
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PubMed id
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Figure 2.
Fig. 2. The manα1–2man-bound rfhSP-D trimer showing the
bound manα1–2man (only the terminal mannose man1 is visible
in the electron density) and the calcium ions (green spheres).
(a) Viewed down the molecular 3-fold axis. (b) Viewed
perpendicular to the molecular 3-fold axis.
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Figure 3.
Fig. 3. The coordination of the calcium ion Ca1 and the bound
ligands in selected subunits of the rfhSP-D–ligand complexes.
(a) Chain B of the inositol phosphate structure. (b) Chain A,
maltose. (c) Chain A, galactose. (d) Chain A, manα1–2man. (e)
Chain B, manα1–4man. (f) Chain A, manα1–4man.
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by Elsevier
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Secondary reference #2
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Title
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High-Resolution structural insights into ligand binding and immune cell recognition by human lung surfactant protein d.
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Authors
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A.K.Shrive,
H.A.Tharia,
P.Strong,
U.Kishore,
I.Burns,
P.J.Rizkallah,
K.B.Reid,
T.J.Greenhough.
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Ref.
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J Mol Biol, 2003,
331,
509-523.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. The maltose-bound rfhSP-D trimer showing the
bound maltose, the three calcium ions and the central asymmetric
tyrosine C228 (generated using MOLSCRIPT.[39.]) (a) Viewed down
the molecular 3-fold; (b) viewed perpendicular to the molecular
3-fold.
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Figure 7.
Figure 7. Stereoviews (maltose-bound structure) of the
neck-CRD interface and interactions. Chain A is in yellow, B in
blue and C in red. (a) The interface between CRD A and neck C
showing the asymmetric residues TyrC228 and LysA229. The
LysC230-GlyA265 contact is present due only to a crystal contact
(see the text). (b) The interface between CRD B and neck A
showing the asymmetric GluB232 (maltose-bound structure only).
The conformation of His220 differs from that in (a) due to a
crystal contact. Figure generated using MOLSCRIPT.[39.]
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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