Journal Home
Search for

Volume 582, Issue 20, Pages 2985-2992 (3 September 2008)


View previous. 4 of 31 View next.

Crystal structure of the IL-22/IL-22R1 complex and its implications for the IL-22 signaling mechanism

Edited by Hans Eklund

Lucas Bleichera, Patricia Ribeiro de Mouraa, Leandra Watanabea, Didier Colaub, Laure Dumoutierbc, Jean-Christophe Renauldbc, Igor PolikarpovaCorresponding Author Informationemail address

Received 13 June 2008; received in revised form 2 July 2008; accepted 6 July 2008. published online 01 August 2008.

Abstract 

Interleukin-22 (IL-22) is a member of the interleukin-10 cytokine family, which is involved in anti-microbial defenses, tissue damage protection and repair, and acute phase responses. Its signaling mechanism involves the sequential binding of IL-22 to interleukin-22 receptor 1 (IL-22R1), and of this dimer to interleukin-10 receptor 2 (IL-10R2) extracellular domain. We report a 1.9Å crystal structure of the IL-22/IL-22R1 complex, revealing crucial interacting residues at the IL-22/IL-22R1 interface. Functional importance of key residues was confirmed by site-directed mutagenesis and functional studies. Based on the X-ray structure of the binary complex, we discuss a molecular basis of the IL-22/IL-22R1 recognition by IL-10R2.

Structured summary


MINT-6693956:

Il22 (uniprotkb:Q9GZX6) and IL22R1 (uniprotkb:Q8N6P7) bind (MI:0407) by X-ray crystallography (MI:0114)

a Instituto de Física de São Carlos, Universidade de São Paulo, Av. Trabalhador São-Carlense, 400, CEP 13560-970 São Carlos, SP, Brazil

b Ludwig Institute for Cancer Research, Brussels Branch, Belgium

c Experimental Medicine Unit, Christian de Duve Institute, Université Catholique de Louvain, Brussels, Belgium

Corresponding Author InformationCorresponding author. Fax: +55 16 33739881.

PII: S0014-5793(08)00647-9

doi:10.1016/j.febslet.2008.07.046


View previous. 4 of 31 View next.