8YWP
Crystal structure of the Fab fragment of anti-IL-6 antibody I9H
Summary for 8YWP
| Entry DOI | 10.2210/pdb8ywp/pdb |
| Descriptor | Heavy chain of the Fab fragment of anti-IL-6 antibody I9H, Light chain of the Fab fragment of anti-IL-6 antibody I9H, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | interleukin, dimer, swap, immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 2 |
| Total formula weight | 48643.38 |
| Authors | Yudenko, A.,Bukhdruker, S.,Eliseev, I.,Rodin, S.,Burtseva, A.,Petrov, A.,Zlobina, O.,Ischenko, A.,Borshchevskiy, V. (deposition date: 2024-03-31, release date: 2024-11-06, Last modification date: 2025-01-15) |
| Primary citation | Yudenko, A.,Bukhdruker, S.,Shishkin, P.,Rodin, S.,Burtseva, A.,Petrov, A.,Pigareva, N.,Sokolov, A.,Zinovev, E.,Eliseev, I.,Remeeva, A.,Marin, E.,Mishin, A.,Gordeliy, V.,Gushchin, I.,Ischenko, A.,Borshchevskiy, V. Structural basis of signaling complex inhibition by IL-6 domain-swapped dimers. Structure, 33:171-180.e5, 2025 Cited by PubMed Abstract: Interleukin-6 (IL-6) is a multifaceted cytokine essential in many immune system processes and their regulation. It also plays a key role in hematopoiesis, and in triggering the acute phase reaction. IL-6 overproduction is critical in chronic inflammation associated with autoimmune diseases like rheumatoid arthritis and contributes to cytokine storms in COVID-19 patients. Over 20 years ago, researchers proposed that IL-6, which is typically monomeric, can also form dimers via a domain-swap mechanism, with indirect evidence supporting their existence. The physiological significance of IL-6 dimers was shown in B-cell chronic lymphocytic leukemia. However, no structures have been reported so far. Here, we present the crystal structure of an IL-6 domain-swapped dimer that computational approaches could not predict. The structure explains why the IL-6 dimer is antagonistic to the IL-6 monomer in signaling complex formation and provides insights for IL-6 targeted therapies. PubMed: 39566503DOI: 10.1016/j.str.2024.10.028 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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