6Z6Y
Galectin-8 N-terminal domain in complex with a sulfatide mimicking a sphingolipid
Summary for 6Z6Y
| Entry DOI | 10.2210/pdb6z6y/pdb |
| Descriptor | 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) |
| Functional Keywords | galectin-8, sphingolipid, cell adhesion |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 18528.01 |
| Authors | Romero, A.,Medrano, F.J. (deposition date: 2020-05-29, release date: 2020-12-30, Last modification date: 2024-01-24) |
| Primary citation | 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 Cited by 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: 33409472DOI: 10.1016/j.isci.2020.101919 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.34 Å) |
Structure validation
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