2rb3
From Proteopedia
Crystal Structure of Human Saposin D
Overview
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.
About this Structure
2RB3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of human saposins C and d: implications for lipid recognition and membrane interactions., Rossmann M, Schultz-Heienbrok R, Behlke J, Remmel N, Alings C, Sandhoff K, Saenger W, Maier T, Structure. 2008 May;16(5):809-17. PMID:18462685 Page seeded by OCA on Thu May 22 22:29:48 2008
Categories: Homo sapiens | Single protein | Maier, T. | Rossman, M. | Saenger, W. | Activator protein | Alternative splicing | Disease mutation | Gaucher disease | Glycoprotein | Gm2-gangliosidosis | Lipid binding protein | Lipid metabolism | Lysosome | Metachromatic leukodystrophy | Sap | Saposin | Sphingolipid metabolism
