Электронный каталог

Статья

Yudenko, A.
Structural Basis of Signaling Complex Inhibition by IL-6 Domain-Swapped Dimers / A.Yudenko, V.Borshchevskiy, [a.o.] // Structure [Electronic resource]. – 2025. – Vol. 33, No. 1. – P. 171-180.e5. – URL: https://doi.org/10.1016/j.str.2024.10.028. – Bibliogr.: 62.

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.



Спец.(статьи,препринты) = 28.0 - Биология$
Спец.(статьи,препринты) = С 44 б - Разделение химических элементов экстракционными и ионообменными методами
ОИЯИ = ОИЯИ (JINR)2025