| pubmed-article:20669242 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20669242 | lifeskim:mentions | umls-concept:C0205182 | lld:lifeskim |
| pubmed-article:20669242 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:20669242 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:20669242 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:20669242 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:20669242 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:20669242 | lifeskim:mentions | umls-concept:C1438051 | lld:lifeskim |
| pubmed-article:20669242 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:20669242 | pubmed:dateCreated | 2010-9-27 | lld:pubmed |
| pubmed-article:20669242 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:abstractText | Post-translational modifications of histone tails are among the most prominent epigenetic marks and play a critical role in transcriptional control at the level of chromatin. The Polycomblike (Pcl) protein is part of a histone methyltransferase complex (Pcl-PRC2) responsible for high levels of histone H3 K27 trimethylation. Studies in Drosophila larvae suggest that Pcl is required for anchoring Pcl-PRC2 at target genes, but how this is achieved is unknown. Pcl comprises a Tudor domain and two PHD fingers. These domains are known to recognize methylated lysine or arginine residues and could contribute to targeting of Pcl-PRC2. Here, we report an NMR structure of the Tudor domain from Drosophila Pcl (Pcl-Tudor) and binding studies with putative ligands. Pcl-Tudor contains an atypical, incomplete aromatic cage that does not interact with known Tudor domain ligands, such as methylated lysines or arginines. Interestingly, human Pcl orthologs exhibit a complete aromatic cage, suggesting that they may recognize methylated lysines. Structural comparison with other Tudor domains suggests that Pcl-Tudor may engage in intra- or intermolecular interactions through an exposed hydrophobic surface patch. | lld:pubmed |
| pubmed-article:20669242 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20669242 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20669242 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20669242 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20669242 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:20669242 | pubmed:issn | 1469-896X | lld:pubmed |
| pubmed-article:20669242 | pubmed:author | pubmed-author:SattlerMichae... | lld:pubmed |
| pubmed-article:20669242 | pubmed:author | pubmed-author:MüllerJürgJ | lld:pubmed |
| pubmed-article:20669242 | pubmed:author | pubmed-author:KlymenkoTetya... | lld:pubmed |
| pubmed-article:20669242 | pubmed:author | pubmed-author:OddoneAnnaA | lld:pubmed |
| pubmed-article:20669242 | pubmed:author | pubmed-author:FribergAnders... | lld:pubmed |
| pubmed-article:20669242 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20669242 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:20669242 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20669242 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20669242 | pubmed:pagination | 1906-16 | lld:pubmed |
| pubmed-article:20669242 | pubmed:dateRevised | 2011-10-3 | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
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| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:meshHeading | pubmed-meshheading:20669242... | lld:pubmed |
| pubmed-article:20669242 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20669242 | pubmed:articleTitle | Structure of an atypical Tudor domain in the Drosophila Polycomblike protein. | lld:pubmed |
| pubmed-article:20669242 | pubmed:affiliation | Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstr. 1, Neuherberg, Germany. | lld:pubmed |
| pubmed-article:20669242 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20669242 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20669242 | lld:entrezgene |
