Crystal structures of saposins A and C
| Autor: | Jean-René Alattia, Paul Leyko, Victoria E. Ahn, Lu Chen, Gilbert G. Privé |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Detergents Molecular Sequence Data Sequence alignment Crystallography X-Ray Biochemistry Article Saposins Polyethylene Glycols Sphingolipid Activator Proteins chemistry.chemical_compound Hydrolase Humans Amino Acid Sequence Protein Structure Quaternary Molecular Biology Peptide sequence chemistry.chemical_classification Chemistry Membrane Enzyme Monomer lipids (amino acids peptides and proteins) Ultracentrifuge Crystallization Dimerization Sequence Alignment Ultracentrifugation Ethers |
| Zdroj: | Protein Science. 15:1849-1857 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1110/ps.062256606 |
| Popis: | Saposins A and C are sphingolipid activator proteins required for the lysosomal breakdown of galactosylceramide and glucosylceramide, respectively. The saposins interact with lipids, leading to an enhanced accessibility of the lipid headgroups to their cognate hydrolases. We have determined the crystal structures of human saposins A and C to 2.0 Angstroms and 2.4 Angstroms, respectively, and both reveal the compact, monomeric saposin fold. We confirmed that these two proteins were monomeric in solution at pH 7.0 by analytical centrifugation. However, at pH 4.8, in the presence of the detergent C(8)E(5), saposin A assembled into dimers, while saposin C formed trimers. Saposin B was dimeric under all conditions tested. The self-association of the saposins is likely to be relevant to how these small proteins interact with lipids, membranes, and hydrolase enzymes. |
| Databáze: | OpenAIRE |
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