Regular ArticleStructural Changes of Surfactant Protein A Induced by Cations Reorient the Protein on Lipid Bilayers☆
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Structural hallmarks of lung surfactant: Lipid-protein interactions, membrane structure and future challenges
2021, Archives of Biochemistry and BiophysicsCitation Excerpt :SP-A and SP-D are hydrophilic, oligomeric and fibrous proteins belonging to the collectin family of proteins. SP-A monomers contain four domains: a N-terminal domain, a collagen-like domain forming a (triple helix) trimeric stem in the quaternary structure, an α-helical connecting region and a C-terminal region containing a carbohydrate recognition domain (CRD) with calcium-binding sites [16]. Six SP-A trimers give rise to an octadecamer where three C-terminal domains form a globular end, thus, with one octadecamer containing six of those globular heads.
The Surfactant System
2019, Kendig's Disorders of the Respiratory Tract in ChildrenThe Surfactant System
2012, Kendig and Chernick's Disorders of the Respiratory Tract in ChildrenComparison of DPPC and DPPG environments in pulmonary surfactant models
2007, Biophysical JournalCitation Excerpt :SP-A has a higher affinity for DPPC than for 1,2-dipalmitoyl-sn-glycero-3-phosphoglycerol (DPPG) (13) but DPPG enhances the ability of SP-A to interact with mixtures of lipids in the presence of Ca2+(17). SP-A has been reported to associate with phosphatidylcholine bilayers via its C-terminal region (18,19) and there is evidence suggesting that SP-A interacts at the corners of bilayer tubules in a unique structure, tubular myelin, that can form in surfactant material (19,20). SP-A also enhances the ability of SP-B to promote uptake of DPPC into monolayers (21).
In defense of the lung: surfactant protein A and surfactant protein D
2006, Current Opinion in Pharmacology
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Polin, R. A.Fox, W. W.
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