| pubmed-article:20944746 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20944746 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:20944746 | lifeskim:mentions | umls-concept:C0034788 | lld:lifeskim |
| pubmed-article:20944746 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:20944746 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:20944746 | pubmed:issue | 7317 | lld:pubmed |
| pubmed-article:20944746 | pubmed:dateCreated | 2010-10-14 | lld:pubmed |
| pubmed-article:20944746 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20944746 | pubmed:abstractText | The pre-T-cell antigen receptor (pre-TCR), expressed by immature thymocytes, has a pivotal role in early T-cell development, including TCR ?-selection, survival and proliferation of CD4(-)CD8(-) double-negative thymocytes, and subsequent ?? T-cell lineage differentiation. Whereas ??TCR ligation by the peptide-loaded major histocompatibility complex initiates T-cell signalling, pre-TCR-induced signalling occurs by means of a ligand-independent dimerization event. The pre-TCR comprises an invariant ?-chain (pre-T?) that pairs with any TCR ?-chain (TCR?) following successful TCR ?-gene rearrangement. Here we provide the basis of pre-T?-TCR? assembly and pre-TCR dimerization. The pre-T? chain comprised a single immunoglobulin-like domain that is structurally distinct from the constant (C) domain of the TCR ?-chain; nevertheless, the mode of association between pre-T? and TCR? mirrored that mediated by the C?-C? domains of the ??TCR. The pre-TCR had a propensity to dimerize in solution, and the molecular envelope of the pre-TCR dimer correlated well with the observed head-to-tail pre-TCR dimer. This mode of pre-TCR dimerization enabled the pre-T? domain to interact with the variable (V) ? domain through residues that are highly conserved across the V? and joining (J) ? gene families, thus mimicking the interactions at the core of the ??TCR's V?-V? interface. Disruption of this pre-T?-V? dimer interface abrogated pre-TCR dimerization in solution and impaired pre-TCR expression on the cell surface. Accordingly, we provide a mechanism of pre-TCR self-association that allows the pre-T? chain to simultaneously 'sample' the correct folding of both the V and C domains of any TCR ?-chain, regardless of its ultimate specificity, which represents a critical checkpoint in T-cell development. This unusual dual-chaperone-like sensing function of pre-T? represents a unique mechanism in nature whereby developmental quality control regulates the expression and signalling of an integral membrane receptor complex. | lld:pubmed |
| pubmed-article:20944746 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20944746 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20944746 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20944746 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20944746 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20944746 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20944746 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20944746 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20944746 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:20944746 | pubmed:issn | 1476-4687 | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:KingGlenn FGF | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:WilliamsNeal... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:GodfreyDale... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:PeruginiMatth... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:WangChristina... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:ChenZhenjunZ | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:McCluskeyJame... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:PangSiew... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:WilceMatthew... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:BeddoeTravisT | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:PurcellAnthon... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:TiganisTonyT | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:La... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:Kjer-NielsenL... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:RossjohnJamie... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:CowiesonNatha... | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:BerryRichardR | lld:pubmed |
| pubmed-article:20944746 | pubmed:author | pubmed-author:ChewSock... | lld:pubmed |
| pubmed-article:20944746 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20944746 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:20944746 | pubmed:volume | 467 | lld:pubmed |
| pubmed-article:20944746 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20944746 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20944746 | pubmed:pagination | 844-8 | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:meshHeading | pubmed-meshheading:20944746... | lld:pubmed |
| pubmed-article:20944746 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20944746 | pubmed:articleTitle | The structural basis for autonomous dimerization of the pre-T-cell antigen receptor. | lld:pubmed |
| pubmed-article:20944746 | pubmed:affiliation | The Protein Crystallography Unit, Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, Victoria 3800, Australia. | lld:pubmed |
| pubmed-article:20944746 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20944746 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20944746 | lld:pubmed |
