| pubmed-article:2904656 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2904656 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2904656 | lifeskim:mentions | umls-concept:C1518803 | lld:lifeskim |
| pubmed-article:2904656 | pubmed:issue | 6199 | lld:pubmed |
| pubmed-article:2904656 | pubmed:dateCreated | 1989-1-18 | lld:pubmed |
| pubmed-article:2904656 | pubmed:abstractText | The POU domain (pronounced 'pow') is a highly charged 155-162-amino-acid (aa) region of sequence similarity contained within three mammalian transcription factors. Pt-1 (ref. 2), Oct-1 (ref. 3) and Oct-2 (ref. 4), and the product of the nematode gene unc-86 (ref. 5) which is involved in determining neural cell lineage. This domain consists of two subdomains, a C-terminal homoeo domain and an N-terminal POU-specific region separated by a short nonconserved linker; the sequence relationship shows that the POU homoeo domains form a distinct POU-related family. In the ubiquitous and lymphoid-specific octamer-motif binding proteins Oct-1 and Oct-2, the POU domain is sufficient for sequence-specific DNA binding. Homoeobox domains contain a helix-turn-helix DNA-binding motif, first identified in bacterial repressors. The helix-turn-helix region of the POU domain is important for DNA binding and, in other classes of homoeo-containing proteins, the entire homoeo domain is sufficient for DNA binding; thus the new POU-specific region could be involved in other functions such as protein-protein interactions. Nevertheless, we show here that in fact the POU domain is a novel bipartite DNA-binding structure in which the POU homoeo and POU-specific regions form two subdomains that are both required for DNA binding but are held together by a flexible linker. | lld:pubmed |
| pubmed-article:2904656 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2904656 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2904656 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2904656 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2904656 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2904656 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2904656 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2904656 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:2904656 | pubmed:author | pubmed-author:HerrWW | lld:pubmed |
| pubmed-article:2904656 | pubmed:author | pubmed-author:SturmR ARA | lld:pubmed |
| pubmed-article:2904656 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2904656 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:2904656 | pubmed:volume | 336 | lld:pubmed |
| pubmed-article:2904656 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2904656 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2904656 | pubmed:pagination | 601-4 | lld:pubmed |
| pubmed-article:2904656 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2904656 | pubmed:meshHeading | pubmed-meshheading:2904656-... | lld:pubmed |
| pubmed-article:2904656 | pubmed:meshHeading | pubmed-meshheading:2904656-... | lld:pubmed |
| pubmed-article:2904656 | pubmed:meshHeading | pubmed-meshheading:2904656-... | lld:pubmed |
| pubmed-article:2904656 | pubmed:meshHeading | pubmed-meshheading:2904656-... | lld:pubmed |
| pubmed-article:2904656 | pubmed:meshHeading | pubmed-meshheading:2904656-... | lld:pubmed |
| pubmed-article:2904656 | pubmed:meshHeading | pubmed-meshheading:2904656-... | lld:pubmed |
| pubmed-article:2904656 | pubmed:meshHeading | pubmed-meshheading:2904656-... | lld:pubmed |
| pubmed-article:2904656 | pubmed:meshHeading | pubmed-meshheading:2904656-... | lld:pubmed |
| pubmed-article:2904656 | pubmed:meshHeading | pubmed-meshheading:2904656-... | lld:pubmed |
| pubmed-article:2904656 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2904656 | pubmed:articleTitle | The POU domain is a bipartite DNA-binding structure. | lld:pubmed |
| pubmed-article:2904656 | pubmed:affiliation | Cold Spring Harbor Laboratory, New York 11724. | lld:pubmed |
| pubmed-article:2904656 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2904656 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2904656 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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