3og4 | pdb_00003og4
The crystal structure of human interferon lambda 1 complexed with its high affinity receptor in space group P21212
Structural highlights
Function[IFNL1_HUMAN] Cytokine with immunomodulatory activity. May play a role in antiviral immunity. Up-regulates MHC class I antigen expression. Ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1. The ligand/receptor complex seems to signal through the Jak-STAT pathway. [INLR1_HUMAN] The IFNLR1/IL10RB dimer is a receptor for IFNL1, IFNL2 and IFNL3. The ligand/receptor complex seems to signal through the Jak-STAT pathway. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium.[1] [2] [3] Publication Abstract from PubMedInterferon (IFN)-lambda1 [also known as interleukin (IL)-29] belongs to the recently discovered group of type III IFNs. All type III IFNs initiate signaling processes through formation of specific heterodimeric receptor complexes consisting of IFN-lambdaR1 and IL-10R2. We have determined the structure of human IFN-lambda1 complexed with human IFN-lambdaR1, a receptor unique to type III IFNs. The overall structure of IFN-lambda1 is topologically similar to the structure of IL-10 and other members of the IL-10 family of cytokines. IFN-lambdaR1 consists of two distinct domains having fibronectin type III topology. The ligand-receptor interface includes helix A, loop AB, and helix F on the IFN site, as well as loops primarily from the N-terminal domain and inter-domain hinge region of IFN-lambdaR1. Composition and architecture of the interface that includes only a few direct hydrogen bonds support an idea that long-range ionic interactions between ligand and receptor govern the process of initial recognition of the molecules while hydrophobic interactions finalize it. Crystal Structure of Human Interferon-lambda1 in Complex with Its High-Affinity Receptor Interferon-lambdaR1.,Miknis Z, Magracheva E, Li W, Zdanov A, Kotenko SV, Wlodawer A J Mol Biol. 2010 Oct 8. PMID:20934432[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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