3OG4

The crystal structure of human interferon lambda 1 complexed with its high affinity receptor in space group P21212

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002829	biological_process	negative regulation of type 2 immune response
A	0005102	molecular_function	signaling receptor binding
A	0005125	molecular_function	cytokine activity
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0007259	biological_process	cell surface receptor signaling pathway via JAK-STAT
A	0008285	biological_process	negative regulation of cell population proliferation
A	0032002	cellular_component	interleukin-28 receptor complex
A	0032003	molecular_function	interleukin-28 receptor binding
A	0032696	biological_process	negative regulation of interleukin-13 production
A	0032714	biological_process	negative regulation of interleukin-5 production
A	0032729	biological_process	positive regulation of type II interferon production
A	0038196	biological_process	type III interferon-mediated signaling pathway
A	0042531	biological_process	positive regulation of tyrosine phosphorylation of STAT protein
A	0043381	biological_process	negative regulation of memory T cell differentiation
A	0045087	biological_process	innate immune response
A	0045345	biological_process	positive regulation of MHC class I biosynthetic process
A	0045581	biological_process	negative regulation of T cell differentiation
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
A	0050778	biological_process	positive regulation of immune response
A	0051607	biological_process	defense response to virus
A	0098586	biological_process	cellular response to virus

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	100
Details	Domain: {"description":"Fibronectin type-III","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20934432","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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