Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved α-helix for Act1 binding and IL-17 signaling
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Title
Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved α-helix for Act1 binding and IL-17 signaling
Authors
Keywords
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Journal
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Volume 70, Issue 5, Pages 1476-1483
Publisher
International Union of Crystallography (IUCr)
Online
2014-05-01
DOI
10.1107/s1399004714005227
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Note: Only part of the references are listed.- The Critical Role of Epithelial-Derived Act1 in IL-17- and IL-25-Mediated Pulmonary Inflammation
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- Features and development ofCoot
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- The IL-17 pathway as a major therapeutic target in autoimmune diseases
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- Signaling of interleukin-17 family cytokines in immunity and inflammation
- (2010) Seon Hee Chang et al. CELLULAR SIGNALLING
- SEF/IL-17R (SEFIR) Is Not Enough
- (2010) Reiko M. Onishi et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- IL-17RC Is Required for Immune Signaling via an Extended SEF/IL-17R Signaling Domain in the Cytoplasmic Tail
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- MolProbity: all-atom structure validation for macromolecular crystallography
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- Th17 cells and IL-17 receptor signaling are essential for mucosal host defense against oral candidiasis
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- IL-17 Signaling-Independent Central Nervous System Autoimmunity Is Negatively Regulated by TGF-
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- Structural basis for antagonism of human interleukin 18 by poxvirus interleukin 18-binding protein
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