Crystal structures of human saposins C and D: implications for lipid recognition and membrane interactions

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Item Type:	Article
Title:	Crystal structures of human saposins C and D: implications for lipid recognition and membrane interactions
Creators Name:	Rossmann, M., Schultz-Heienbrok, R., Behlke, J., Remmel, N., Alings, C., Sandhoff, K., Saenger, W. and Maier, T.
Abstract:	Human saposins are essential proteins required for degradation of sphingolipids and lipid antigen presentation. Despite the conserved structural organization of saposins, their distinct modes of interaction with biological membranes are not fully understood. We describe two crystal structures of human saposin C in an "open" configuration with unusual domain swapped homodimers. This form of SapC dimer supports the "clip-on" model for SapC-induced vesicle fusion. In addition, we present the crystal structure of SapD in two crystal forms. They reveal the monomer-monomer interface for the SapD dimer, which was confirmed in solution by analytical ultracentrifugation. The crystal structure of SapD suggests that side chains of Lys10 and Arg17 are involved in initial association with the preferred anionic biological membranes by forming salt bridges with sulfate or phosphate lipid headgroups.
Keywords:	Proteins, CELLBIO
Source:	Structure
ISSN:	0969-2126
Publisher:	Cell Press
Volume:	16
Number:	5
Page Range:	809-817
Date:	7 May 2008
Official Publication:	https://doi.org/10.1016/j.str.2008.02.016
PubMed:	View item in PubMed

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