1Y6K

Crystal structure of human IL-10 complexed with the soluble IL-10R1 chain

Summary for 1Y6K

• Entry DOI: 10.2210/pdb1y6k/pdb
• Related: 1J7V 1Y6M 1Y6N
• Descriptor: Interleukin-10, Interleukin-10 receptor alpha chain (3 entities in total)
• Functional Keywords: helix bundle, receptor complex, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P22301; Membrane; Single-pass type I membrane protein: Q13651
• Total number of polymer chains: 2
• Total formula weight: 43179.00

Authors

Yoon, S.I.,Jones, B.C.,Josepson, K.,Logsdon, N.J.,Walter, M.R. (deposition date: 2004-12-06, release date: 2005-12-20, Last modification date: 2024-10-09)

Primary citation

Yoon, S.I.,Jones, B.C.,Logsdon, N.J.,Walter, M.R.
Same structure, different function crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain.
Structure, 13:551-564, 2005

PubMed Abstract: Human IL-10 (hIL-10) is a cytokine that modulates diverse immune responses. The Epstein-Barr virus (EBV) genome contains an IL-10 homolog (vIL-10) that shares high sequence and structural similarity with hIL-10. Although vIL-10 suppresses inflammatory responses like hIL-10, it cannot activate many other immunostimulatory functions performed by the cellular cytokine. These functional differences have been correlated with the approximately 1000-fold lower affinity of vIL-10, compared to hIL-10, for the IL-10R1 receptor chain. To define the structural basis for these observations, crystal structures of vIL-10 and a vIL-10 point mutant were determined bound to the soluble IL-10R1 receptor fragment (sIL-10R1) at 2.8 and 2.7 A resolution, respectively. The structures reveal that subtle changes in the conformation and dynamics of the vIL-10 AB and CD loops and an orientation change of vIL-10 on sIL-10R1 are the main factors responsible for vIL-10's reduced affinity for sIL-10R1 and its distinct biological profile.

PubMed: 15837194
DOI: 10.1016/j.str.2005.01.016

Experimental method

X-RAY DIFFRACTION (2.52 Å)