| pubmed-article:20934432 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20934432 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:20934432 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:20934432 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:20934432 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:20934432 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:20934432 | pubmed:dateCreated | 2010-11-24 | lld:pubmed |
| pubmed-article:20934432 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20934432 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20934432 | pubmed:abstractText | Interferon (IFN)-?1 [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-?R1 and IL-10R2. We have determined the structure of human IFN-?1 complexed with human IFN-?R1, a receptor unique to type III IFNs. The overall structure of IFN-?1 is topologically similar to the structure of IL-10 and other members of the IL-10 family of cytokines. IFN-?R1 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-?R1. 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. | lld:pubmed |
| pubmed-article:20934432 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20934432 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20934432 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20934432 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20934432 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20934432 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20934432 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20934432 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20934432 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:20934432 | pubmed:issn | 1089-8638 | lld:pubmed |
| pubmed-article:20934432 | pubmed:author | pubmed-author:FuY PYP | lld:pubmed |
| pubmed-article:20934432 | pubmed:author | pubmed-author:WlodawerAlexa... | lld:pubmed |
| pubmed-article:20934432 | pubmed:author | pubmed-author:KotenkoSergei... | lld:pubmed |
| pubmed-article:20934432 | pubmed:author | pubmed-author:ZdanovAlexand... | lld:pubmed |
| pubmed-article:20934432 | pubmed:author | pubmed-author:MagrachevaEug... | lld:pubmed |
| pubmed-article:20934432 | pubmed:author | pubmed-author:MiknisZachary... | lld:pubmed |
| pubmed-article:20934432 | pubmed:copyrightInfo | Copyright © 2010 Elsevier Ltd. All rights reserved. | lld:pubmed |
| pubmed-article:20934432 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20934432 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:20934432 | pubmed:volume | 404 | lld:pubmed |
| pubmed-article:20934432 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20934432 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20934432 | pubmed:pagination | 650-64 | lld:pubmed |
| pubmed-article:20934432 | pubmed:dateRevised | 2011-10-6 | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:meshHeading | pubmed-meshheading:20934432... | lld:pubmed |
| pubmed-article:20934432 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20934432 | pubmed:articleTitle | Crystal structure of human interferon-?1 in complex with its high-affinity receptor interferon-?R1. | lld:pubmed |
| pubmed-article:20934432 | pubmed:affiliation | Macromolecular Crystallography Laboratory, NCI-Frederick, Frederick, MD 21702, USA. | lld:pubmed |
| pubmed-article:20934432 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20934432 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:20934432 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| pubmed-article:20934432 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20934432 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20934432 | lld:entrezgene |
