2GTG
Crystal Structure of Human Saposin C
Summary for 2GTG
| Entry DOI | 10.2210/pdb2gtg/pdb |
| Related | 1M12 1N69 2DOB |
| Descriptor | Proactivator polypeptide (2 entities in total) |
| Functional Keywords | saposin, sphingolipid activator protein, lipid-binding protein, lipid binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Lysosome: P07602 |
| Total number of polymer chains | 1 |
| Total formula weight | 9305.69 |
| Authors | Prive, G.G.,Ahn, V.E. (deposition date: 2006-04-28, release date: 2006-07-25, Last modification date: 2024-10-30) |
| Primary citation | Ahn, V.E.,Leyko, P.,Alattia, J.R.,Chen, L.,Prive, G.G. Crystal structures of saposins A and C. Protein Sci., 15:1849-1857, 2006 Cited by PubMed Abstract: 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. PubMed: 16823039DOI: 10.1110/ps.062256606 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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