2h24
From Proteopedia
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Crystal structure of human IL-10
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Graft-versus-host disease, protection against OMIM:[124092], HIV-1, susceptibility to OMIM:[124092], Rheumatoid arthritis, progression of OMIM:[124092]
About this Structure
2H24 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex., Yoon SI, Logsdon NJ, Sheikh F, Donnelly RP, Walter MR, J Biol Chem. 2006 Nov 17;281(46):35088-96. Epub 2006 Sep 18. PMID:16982608
Page seeded by OCA on Mon Nov 12 22:24:59 2007
