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2DOB

Crystal Structure of Human Saposin A

Summary for 2DOB
Entry DOI10.2210/pdb2dob/pdb
Related1M12 1N69 2GTG
DescriptorProactivator polypeptide, CALCIUM ION (3 entities in total)
Functional Keywordssaposin, sphingolipid activator protein, lipid-binding protein, lipid binding protein
Biological sourceHomo sapiens (human)
Cellular locationLysosome: P07602
Total number of polymer chains1
Total formula weight9242.26
Authors
Prive, G.G.,Ahn, V.E. (deposition date: 2006-04-28, release date: 2006-07-25, Last modification date: 2024-11-13)
Primary citationAhn, 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: 16823039
DOI: 10.1110/ps.062256606
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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