Title : Crystal structure of human
interferon-λ1 in complex with its high-affinity
receptor interferon-λR1
Abstract :
- Interferon ( IFN)-λ1 [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-λR1 and IL-10R2
- We have determined the structure of human IFN-λ1 complexed with human IFN-λR1 , a receptor unique to type III IFNs
- The overall structure of IFN-λ1 is topologically similar to the structure of IL-10 and other members of the IL-10 family of cytokines
- IFN-λR1 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-λR1
- Com position 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
Output (sent_index, trigger,
protein,
sugar,
site):
Output(Part-Of) (sent_index,
protein,
site):
- 6. IFN-λR1, domain
- 6. IFN-λR1, region
- 6. IFN, site
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):