| pubmed-article:19654330 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19654330 | lifeskim:mentions | umls-concept:C0042172 | lld:lifeskim |
| pubmed-article:19654330 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:19654330 | lifeskim:mentions | umls-concept:C2825045 | lld:lifeskim |
| pubmed-article:19654330 | lifeskim:mentions | umls-concept:C1853126 | lld:lifeskim |
| pubmed-article:19654330 | lifeskim:mentions | umls-concept:C1416687 | lld:lifeskim |
| pubmed-article:19654330 | pubmed:issue | 40 | lld:pubmed |
| pubmed-article:19654330 | pubmed:dateCreated | 2009-10-5 | lld:pubmed |
| pubmed-article:19654330 | pubmed:abstractText | The killer cell lectin-like receptor G1, KLRG1, is a cell surface receptor expressed on subsets of natural killer (NK) cells and T cells. KLRG1 was recently found to recognize E-cadherin and thus inhibit immune responses by regulating the effector function and the developmental processes of NK and T cells. E-cadherin is expressed on epithelial cells and exhibits Ca(2+)-dependent homophilic interactions that contribute to cell-cell junctions. However, the mechanism underlying the molecular recognition of KLRG1 by E-cadherin remains unclear. Here, we report structural, binding, and functional analyses of this interaction using multiple methods. Surface plasmon resonance demonstrated that KLRG1 binds the E-cadherin N-terminal domains 1 and 2 with low affinity (K(d) approximately 7-12 microm), typical of cell-cell recognition receptors. NMR binding studies showed that only a limited N-terminal region of E-cadherin, comprising the homodimer interface, exhibited spectrum perturbation upon KLRG1 complex formation. It was confirmed by binding studies using a series of E-cadherin mutants. Furthermore, killing assays using KLRG1(+)NK cells and reporter cell assays demonstrated the functional significance of the N-terminal region of E-cadherin. These results suggest that KLRG1 recognizes the N-terminal homodimeric interface of domain 1 of E-cadherin and binds only the monomeric form of E-cadherin to inhibit the immune response. This raises the possibility that KLRG1 detects monomeric E-cadherin at exposed cell surfaces to control the activation threshold of NK and T cells. | lld:pubmed |
| pubmed-article:19654330 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19654330 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19654330 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19654330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19654330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19654330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19654330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19654330 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19654330 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:19654330 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:YamamotoKazuo... | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:IkuraMitsuhik... | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:ItoMasayukiM | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:MatsumotoNaok... | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:SasakiKaoriK | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:OhkiIzuruI | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:MaenakaKatsum... | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:KurokiKimikoK | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:MaruyamaTakum... | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:KajikawaMizuh... | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:NakamuraSeiko... | lld:pubmed |
| pubmed-article:19654330 | pubmed:author | pubmed-author:KamedaYosukeY | lld:pubmed |
| pubmed-article:19654330 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19654330 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:19654330 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:19654330 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19654330 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19654330 | pubmed:pagination | 27327-35 | lld:pubmed |
| pubmed-article:19654330 | pubmed:dateRevised | 2010-10-5 | lld:pubmed |
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| pubmed-article:19654330 | pubmed:meshHeading | pubmed-meshheading:19654330... | lld:pubmed |
| pubmed-article:19654330 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19654330 | pubmed:articleTitle | Molecular basis for E-cadherin recognition by killer cell lectin-like receptor G1 (KLRG1). | lld:pubmed |
| pubmed-article:19654330 | pubmed:affiliation | Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. | lld:pubmed |
| pubmed-article:19654330 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19654330 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:12550 | entrezgene:pubmed | pubmed-article:19654330 | lld:entrezgene |
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| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19654330 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19654330 | lld:entrezgene |
