6Z6Y

Galectin-8 N-terminal domain in complex with a sulfatide mimicking a sphingolipid

6Z6Y の概要

• エントリーDOI: 10.2210/pdb6z6y/pdb
• 分子名称: Galectin-8, [(2~{R},3~{R},4~{S},5~{S},6~{R})-2-[(2~{S})-2-acetamido-3-oxidanylidene-pent-4-enoxy]-6-(hydroxymethyl)-3,5-bis(oxidanyl)oxan-4-yl] hydrogen sulfate, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: galectin-8, sphingolipid, cell adhesion
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18528.01

構造登録者

Romero, A.,Medrano, F.J. (登録日: 2020-05-29, 公開日: 2020-12-30, 最終更新日: 2024-01-24)

主引用文献

Murphy, P.V.,Romero, A.,Xiao, Q.,Ludwig, A.K.,Jogula, S.,Shilova, N.V.,Singh, T.,Gabba, A.,Javed, B.,Zhang, D.,Medrano, F.J.,Kaltner, H.,Kopitz, J.,Bovin, N.V.,Wu, A.M.,Klein, M.L.,Percec, V.,Gabius, H.J.
Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes.
Iscience, 24:101919-101919, 2021

PubMed Abstract: The small 3--sulfated galactose head group of sulfatides, an abundant glycosphingolipid class, poses the (sphinx-like) riddle on involvement of glycan bridging by tissue lectins (sugar code). First, synthesis of head group derivatives for functionalization of amphiphilic dendrimers is performed. Aggregation of resulting (biomimetic) vesicles, alone or in combination with lactose, demonstrates bridging by a tissue lectin (galectin-4). Physiologically, this can stabilize glycolipid-rich microdomains (rafts) and associate sulfatide-rich regions with specific glycoproteins. Further testing documents importance of heterobivalency and linker length. Structurally, sulfatide recognition by galectin-8 is shown to involve sphingosine's OH group as substitute for the 3'-hydroxyl of glucose of lactose. These discoveries underscore functionality of this small determinant on biomembranes intracellularly and on the cell surface. Moreover, they provide a role model to examine counterreceptor capacity of more complex glycans of glycosphingolipids and to start their bottom-up glycotope surface programming.

PubMed: 33409472
DOI: 10.1016/j.isci.2020.101919

実験手法

X-RAY DIFFRACTION (1.34 Å)