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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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PDB id:
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| Name: |
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Sugar binding protein
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Title:
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Crystal structure of haemophilus eagan 4a polysaccharide bound human lung surfactant protein d
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Structure:
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Pulmonary surfactant-associated protein d. Chain: a, b, c. Fragment: carbohydrate recognition domain. Synonym: psp-d, sp-d, collectin-7, lung surfactant protein d. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: sftpd, colec7, pspd, sftp4. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.70Å
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R-factor:
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0.192
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R-free:
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0.210
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Authors:
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A.K.Shrive,T.J.Greenhough
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Key ref:
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H.W.Clark
et al.
(2016).
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.
Infect Immun,
84,
1585-1592.
PubMed id:
DOI:
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Date:
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13-Mar-12
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Release date:
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27-Mar-13
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PROCHECK
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Headers
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References
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P35247
(SFTPD_HUMAN) -
Pulmonary surfactant-associated protein D from Homo sapiens
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Seq:
Struc:
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375 a.a.
152 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Infect Immun
84:1585-1592
(2016)
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PubMed id:
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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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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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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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