Structure of IL-33 and Its Interaction with the ST2 and IL-1RAcP ReceptorsInsight into Heterotrimeric IL-1 Signaling Complexes Export

@article{citeulike:5999147, abstract = {Members of the interleukin-1 (IL-1) family of cytokines play major roles in host defense and immune system regulation in infectious and inflammatory diseases. IL-1 cytokines trigger a biological response in effector cells by assembling a heterotrimeric signaling complex with two IL-1 receptor chains, a high-affinity primary receptor and a low-affinity coreceptor. To gain insights into the signaling mechanism of the novel IL-1-like cytokine IL-33, we first solved its solution structure and then performed a detailed biochemical and structural characterization of the interaction between IL-33, its primary receptor ST2, and the coreceptor IL-1RAcP. Using nuclear magnetic resonance data, we obtained a model of the IL-33/ST2 complex in solution that is validated by small-angle X-ray scattering (SAXS) data and is similar to the IL-1²/IL-1R1 complex. We extended our SAXS analysis to the IL-33/ST2/IL-1RAcP and IL-1²/IL-1R1/IL-1RAcP complexes and propose a general model of the molecular architecture of IL-1 ternary signaling complexes.}, author = {Lingel, Andreas and Weiss, Thomas M. and Niebuhr, Marc and Pan, Borlan and Appleton, Brent A. and Wiesmann, Christian and Bazan, J. Fernando and Fairbrother, Wayne J.}, citeulike-article-id = {5999147}, citeulike-linkout-0 = {http://www.cell.com/structure/abstract/S0969-2126(09)00331-1}, day = {14}, keywords = {cytokine, il-1, protein\_structure}, month = {October}, number = {10}, pages = {1398--1410}, posted-at = {2009-10-24 09:31:56}, priority = {2}, title = {Structure of IL-33 and Its Interaction with the ST2 and IL-1RAcP ReceptorsInsight into Heterotrimeric IL-1 Signaling Complexes}, url = {http://www.cell.com/structure/abstract/S0969-2126(09)00331-1}, volume = {17}, year = {2009} }

TY - JOUR ID - citeulike:5999147 L3 - citeulike-article-id:5999147 N2 - Members of the interleukin-1 (IL-1) family of cytokines play major roles in host defense and immune system regulation in infectious and inflammatory diseases. IL-1 cytokines trigger a biological response in effector cells by assembling a heterotrimeric signaling complex with two IL-1 receptor chains, a high-affinity primary receptor and a low-affinity coreceptor. To gain insights into the signaling mechanism of the novel IL-1-like cytokine IL-33, we first solved its solution structure and then performed a detailed biochemical and structural characterization of the interaction between IL-33, its primary receptor ST2, and the coreceptor IL-1RAcP. Using nuclear magnetic resonance data, we obtained a model of the IL-33/ST2 complex in solution that is validated by small-angle X-ray scattering (SAXS) data and is similar to the IL-1²/IL-1R1 complex. We extended our SAXS analysis to the IL-33/ST2/IL-1RAcP and IL-1²/IL-1R1/IL-1RAcP complexes and propose a general model of the molecular architecture of IL-1 ternary signaling complexes. IS - 10 EP - 1410 TI - Structure of IL-33 and Its Interaction with the ST2 and IL-1RAcP ReceptorsInsight into Heterotrimeric IL-1 Signaling Complexes VL - 17 SP - 1398 KW - cytokine KW - il-1 KW - protein_structure AU - Lingel, Andreas AU - Weiss, Thomas AU - Niebuhr, Marc AU - Pan, Borlan AU - Appleton, Brent AU - Wiesmann, Christian AU - Bazan, Fernando AU - Fairbrother, Wayne PY - 2009/10/14/ UR - http://www.cell.com/structure/abstract/S0969-2126(09)00331-1 ER -