9O6N
Structure of Siglec-10
Summary for 9O6N
| Entry DOI | 10.2210/pdb9o6n/pdb |
| Descriptor | Sialic acid-binding Ig-like lectin 10, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CITRATE ANION, ... (7 entities in total) |
| Functional Keywords | siglec, receptor, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 3 |
| Total formula weight | 75723.96 |
| Authors | Medina, E.,Ming, Q.,Tran, T.H.,Luca, V.C. (deposition date: 2025-04-14, release date: 2026-02-25, Last modification date: 2026-09-09) |
| Primary citation | Medina, E.,Mason, C.,Tran, T.H.,Julia, E.P.,Ming, Q.,Taibi, L.M.,Hwu, P.,Maute, R.L.,Burg, J.S.,Luca, V.C. Structural basis for sialoglycan recognition by the immune inhibitory receptor Siglec-10. Structure, 34:768-777.e5, 2026 Cited by PubMed Abstract: Sialic acid-binding immunoglobulin-like lectin 10 (Siglec-10) inhibits immune cell function by sensing the presence of sialylated glycoproteins. Here, we determined structures of Siglec-10 bound to sialyllactose (SL) ligands to visualize the molecular recognition events underlying Siglec-10 signaling. The structures reveal that domain 1 (D1) of Siglec-10 engages SL using a non-conserved, selectivity determining CC' loop. Siglec-10 binds α2,3- and α2,6-linked SL with similar affinities despite minor additional contacts between D1 and the α2,3-SL galactose. Homodimerization of Siglec-10 is mediated by a hydrophobic domain 2 (D2) interface, and mutation of this interface ablates cellular binding similarly to mutations in the CC' loop and glycan-binding site. Surprisingly, knockout of the putative Siglec-10 ligand, CD24, did not affect binding to breast cancer cells, indicating that Siglec-10 has a broader-than-expected glycoprotein recognition profile. These findings emphasize how a complex interplay between Siglec-10 multimerization and ligand engagement facilitate cell surface interactions. PubMed: 41747717DOI: 10.1016/j.str.2026.01.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.98 Å) |
Structure validation
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