4DN8
Structure of porcine surfactant protein D neck and carbohydrate recognition domain complexed with mannose
Summary for 4DN8
| Entry DOI | 10.2210/pdb4dn8/pdb |
| Descriptor | Pulmonary surfactant-associated protein D, CALCIUM ION, beta-D-mannopyranose, ... (4 entities in total) |
| Functional Keywords | collectin, lectin, carbohydrate/sugar binding, lung surfactant, sugar binding protein |
| Biological source | Sus scrofa (pigs,swine,wild boar) |
| Total number of polymer chains | 1 |
| Total formula weight | 17318.31 |
| Authors | van Eijk, M.,Rynkiewicz, M.J.,White, M.R.,Hartshorn, K.L.,Zou, X.,Schulten, K.,Luo, D.,Crouch, E.C.,Cafarella, T.M.,Head, J.F.,Haagsman, H.P.,Seaton, B.A. (deposition date: 2012-02-08, release date: 2012-06-20, Last modification date: 2024-11-20) |
| Primary citation | van Eijk, M.,Rynkiewicz, M.J.,White, M.R.,Hartshorn, K.L.,Zou, X.,Schulten, K.,Luo, D.,Crouch, E.C.,Cafarella, T.R.,Head, J.F.,Haagsman, H.P.,Seaton, B.A. A Unique Sugar-binding Site Mediates the Distinct Anti-influenza Activity of Pig Surfactant Protein D. J.Biol.Chem., 287:26666-26677, 2012 Cited by PubMed Abstract: 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. PubMed: 22685299DOI: 10.1074/jbc.M112.368571 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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