| Innate Immunity | |
| Review: Structural determinants of pattern recognition by lung collectins: | |
| Barbara A.Seaton1  | |
| 关键词: X-ray crystallography; pattern recognition; SP-A; SP-D; lung collectins; | |
| DOI : 10.1177/1753425910368716 | |
| 学科分类:生物科学(综合) | |
| 来源: Sage Journals | |
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【 摘 要 】
Host defense roles for the lung collectins, surfactant protein A (SP-A) and surfactant protein D (SP-D), were first suspected in the 1980s when molecular characterization revealed their sequence homology to the acute phase reactant of serum, mannose-binding lectin. Surfactant protein A and SP-D have since been shown to play diverse and important roles in innate immunity and pulmonary homeostasis. Their location in surfactant ideally positions them to interact with air-space pathogens. Despite extensive structural similarity, the two proteins show many functional differences and considerable divergence in their interactions with microbial surface components, surfactant lipids, and other ligands. Recent crystallographic studies have provided many new insights relating to these observed differences. Although both proteins can participate in calcium-dependent interactions with sugars and other polyols, they display significant differences in the spatial orientation, charge, and hydrophobicity of their binding...
【 授权许可】
CC BY
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201904021005941ZK.pdf | 189KB |
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