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2R0R

Crystal Structure of Human Saposin D variant SapD K9E

Summary for 2R0R
Entry DOI10.2210/pdb2r0r/pdb
Related2QYP 2R1Q 2RB3 2Z9A
DescriptorProactivator polypeptide, SULFATE ION (3 entities in total)
Functional Keywordslipid binding protein, saposin, activator protein, sap, alternative splicing, disease mutation, gaucher disease, glycoprotein, gm2-gangliosidosis, lipid metabolism, lysosome, metachromatic leukodystrophy, sphingolipid metabolism
Biological sourceHomo sapiens (human)
Cellular locationLysosome . Prosaposin: Secreted : P07602
Total number of polymer chains2
Total formula weight19404.24
Authors
Rossmann, M.,Saenger, W.,Maier, T. (deposition date: 2007-08-21, release date: 2008-04-29, Last modification date: 2021-10-20)
Primary citationRossmann, M.,Schultz-Heienbrok, R.,Behlke, J.,Remmel, N.,Alings, C.,Sandhoff, K.,Saenger, W.,Maier, T.
Crystal structures of human saposins C and d: implications for lipid recognition and membrane interactions.
Structure, 16:809-817, 2008
Cited by
PubMed 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.
PubMed: 18462685
DOI: 10.1016/j.str.2008.02.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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数据于2024-10-30公开中

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