NDLI: Structure–function correlations of pulmonary surfactant protein SP-B and the saposin-like family of proteins

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A comparative study of structures and structural transitions of secondary transporters with the LeuT fold

Structure-based statistical analysis of transmembrane helices

Structure–function correlations of pulmonary surfactant protein SP-B and the saposin-like family of proteins

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Structure–function correlations of pulmonary surfactant protein SP-B and the saposin-like family of proteins

Content Provider	Springer Nature Link
Author	Olmeda, Bárbara García Álvarez, Begoña Pérez Gil, Jesús
Copyright Year	2012
Abstract	Pulmonary surfactant is a lipid-protein complex secreted by the respiratory epithelium of mammalian lungs, which plays an essential role in stabilising the alveolar surface and so reducing the work of breathing. The surfactant protein SP-B is part of this complex, and is strictly required for the assembly of pulmonary surfactant and its extracellular development to form stable surface-active films at the air–liquid alveolar interface, making the lack of SP-B incompatible with life. In spite of its physiological importance, a model for the structure and the mechanism of action of SP-B is still needed. The sequence of SP-B is homologous to that of the saposin-like family of proteins, which are membrane-interacting polypeptides with apparently diverging activities, from the co-lipase action of saposins to facilitate the degradation of sphingolipids in the lysosomes to the cytolytic actions of some antibiotic proteins, such as NK-lysin and granulysin or the amoebapore of Entamoeba histolytica. Numerous studies on the interactions of these proteins with membranes have still not explained how a similar sequence and a potentially related fold can sustain such apparently different activities. In the present review, we have summarised the most relevant features of the structure, lipid-protein and protein–protein interactions of SP-B and the saposin-like family of proteins, as a basis to propose an integrated model and a common mechanistic framework of the apparent functional versatility of the saposin fold.
Starting Page	209
Ending Page	222
Page Count	14
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	42
Issue Number	2-3
e-ISSN	14321017
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-09-21
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Pulmonary surfactant Saposin Amphipathic helices Surface tension Air–liquid interface Lipid-protein interactions Biochemistry Biophysics and Biological Physics Cell Biology Neurobiology Membrane Biology Nanotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

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