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| | ==Structure of porcine surfactant protein D neck and carbohydrate recognition domain complexed with mannose== | | ==Structure of porcine surfactant protein D neck and carbohydrate recognition domain complexed with mannose== |
| - | <StructureSection load='4dn8' size='340' side='right' caption='[[4dn8]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4dn8' size='340' side='right'caption='[[4dn8]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dn8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DN8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DN8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dn8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DN8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SFTPD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SFTPD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dn8 OCA], [http://pdbe.org/4dn8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dn8 RCSB], [http://www.ebi.ac.uk/pdbsum/4dn8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dn8 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dn8 OCA], [https://pdbe.org/4dn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dn8 RCSB], [https://www.ebi.ac.uk/pdbsum/4dn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dn8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SFTPD_PIG SFTPD_PIG]] Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties (By similarity). | + | [[https://www.uniprot.org/uniprot/SFTPD_PIG SFTPD_PIG]] Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Pig]] | | [[Category: Pig]] |
| | [[Category: Cafarella, T M]] | | [[Category: Cafarella, T M]] |
| Structural highlights
Function
[SFTPD_PIG] Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties (By similarity).
Publication Abstract from PubMed
Pigs can act as intermediate hosts by which reassorted influenza A virus (IAV) strains can be transmitted to humans and cause pandemic influenza outbreaks. The innate host defense component surfactant protein D (SP-D) interacts with glycans on the hemagglutinin of IAV and contributes to protection against IAV infection in mammals. This study shows that a recombinant trimeric neck lectin fragment derived from porcine SP-D (pSP-D) exhibits profound inhibitory activity against IAV, in contrast to comparable fragments derived from human SP-D. Crystallographic analysis of the pSP-D fragment complexed with a viral sugar component shows that a unique tripeptide loop alters the lectin site conformation of pSP-D. Molecular dynamics simulations highlight the role of this flexible loop, which adopts a more stable conformation upon sugar binding and may facilitate binding to viral glycans through contact with distal portions of the branched mannoside. The combined data demonstrate that porcine-specific structural features of SP-D contribute significantly to its distinct anti-IAV activity. These findings could help explain why pigs serve as important reservoirs for newly emerging pathogenic IAV strains.
A Unique Sugar-binding Site Mediates the Distinct Anti-influenza Activity of Pig Surfactant Protein D.,van Eijk M, Rynkiewicz MJ, White MR, Hartshorn KL, Zou X, Schulten K, Luo D, Crouch EC, Cafarella TR, Head JF, Haagsman HP, Seaton BA J Biol Chem. 2012 Aug 3;287(32):26666-77. Epub 2012 Jun 8. PMID:22685299[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Eijk M, Rynkiewicz MJ, White MR, Hartshorn KL, Zou X, Schulten K, Luo D, Crouch EC, Cafarella TR, Head JF, Haagsman HP, Seaton BA. A Unique Sugar-binding Site Mediates the Distinct Anti-influenza Activity of Pig Surfactant Protein D. J Biol Chem. 2012 Aug 3;287(32):26666-77. Epub 2012 Jun 8. PMID:22685299 doi:10.1074/jbc.M112.368571
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