2H24

Crystal structure of human IL-10

Summary for 2H24

• Entry DOI: 10.2210/pdb2h24/pdb
• Related: 1INR
• Descriptor: Interleukin-10 (2 entities in total)
• Functional Keywords: alpha-helix bundle, cytokine
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P22301
• Total number of polymer chains: 1
• Total formula weight: 18672.45

Authors

Yoon, S.I.,Walter, M.R. (deposition date: 2006-05-18, release date: 2006-10-17, Last modification date: 2024-11-20)

Primary citation

Yoon, S.I.,Logsdon, N.J.,Sheikh, F.,Donnelly, R.P.,Walter, M.R.
Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex.
J.Biol.Chem., 281:35088-35096, 2006

PubMed Abstract: Interleukin-10 receptor 2 (IL-10R2) is a critical component of the IL-10.IL-10R1.IL-10R2 complex which regulates IL-10-mediated immunomodulatory responses. The ternary IL-10 signaling complex is assembled in a sequential order with the IL-10.IL-10R1 interaction occurring first followed by engagement of the IL-10R2 chain. In this study we map the IL-10R2 binding site on IL-10 using surface plasmon resonance and cell-based assays. Critical IL-10R2 binding residues are located in helix A adjacent to the previously identified IL-10R1 recognition surface. Interestingly, IL-10R2 binding residues located in the N-terminal end of helix A exhibit large structural differences between unbound cIL-10 and cIL-10.IL-10R1 crystal structures. This suggests IL-10R1-induced conformational changes regulate IL-10R2 binding and assembly of the ternary IL-10.IL-10R1.IL-10R2 complex. The basic mechanistic features of the assembly process are likely shared by six additional class-2 cytokines (viral IL-10s, IL-22, IL-26, IL-28A, IL28B, and IL-29) to promote IL-10R2 binding to six additional receptor complexes. These studies highlight the importance of structure in regulating low affinity protein-protein interactions and IL-10 signal transduction.

PubMed: 16982608
DOI: 10.1074/jbc.M606791200

Experimental method

X-RAY DIFFRACTION (2 Å)