2DOB

Crystal Structure of Human Saposin A

2DOB の概要

• エントリーDOI: 10.2210/pdb2dob/pdb
• 関連するPDBエントリー: 1M12 1N69 2GTG
• 分子名称: Proactivator polypeptide, CALCIUM ION (3 entities in total)
• 機能のキーワード: saposin, sphingolipid activator protein, lipid-binding protein, lipid binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Lysosome: P07602
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9242.26

構造登録者

Prive, G.G.,Ahn, V.E. (登録日: 2006-04-28, 公開日: 2006-07-25, 最終更新日: 2024-11-13)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2 Å)