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

Rossmann, M. and Schultz-Heienbrok, R. and Behlke, J. and Remmel, N. and Alings, C. and Sandhoff, K. and Saenger, W. and Maier, T.. (2008) Crystal structures of human saposins C and D: Implications for lipid recognition and membrane interactions. Structure, 16 (5). pp. 809-817.

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Official URL: http://edoc.unibas.ch/45840/

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Cell Press
ISSN:0969-2126
e-ISSN:1878-4186
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:29 Nov 2017 07:24
Deposited On:29 Nov 2017 07:24

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