| pubmed-article:9630226 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9630226 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:9630226 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:9630226 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:9630226 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9630226 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:9630226 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:9630226 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:9630226 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
| pubmed-article:9630226 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9630226 | pubmed:dateCreated | 1998-7-6 | lld:pubmed |
| pubmed-article:9630226 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9630226 | pubmed:abstractText | The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 A resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFkappaB and the p53 tumor suppressor protein. The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other. The phosphotyrosine-binding site of the SH2 domain in each monomer is coupled structurally to the DNA-binding domain, suggesting a potential role for the SH2-phosphotyrosine interaction in the stabilization of DNA interacting elements. | lld:pubmed |
| pubmed-article:9630226 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9630226 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9630226 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9630226 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9630226 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9630226 | pubmed:month | May | lld:pubmed |
| pubmed-article:9630226 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:9630226 | pubmed:author | pubmed-author:DarnellJ... | lld:pubmed |
| pubmed-article:9630226 | pubmed:author | pubmed-author:ChewAA | lld:pubmed |
| pubmed-article:9630226 | pubmed:author | pubmed-author:ZhaiSS | lld:pubmed |
| pubmed-article:9630226 | pubmed:author | pubmed-author:KuriyanJJ | lld:pubmed |
| pubmed-article:9630226 | pubmed:author | pubmed-author:VinkemeierUU | lld:pubmed |
| pubmed-article:9630226 | pubmed:author | pubmed-author:JeruzalmiDD | lld:pubmed |
| pubmed-article:9630226 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9630226 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:9630226 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:9630226 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9630226 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9630226 | pubmed:pagination | 827-39 | lld:pubmed |
| pubmed-article:9630226 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9630226 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9630226 | pubmed:articleTitle | Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. | lld:pubmed |
| pubmed-article:9630226 | pubmed:affiliation | The Rockefeller University, New York, New York 10021, USA. | lld:pubmed |
| pubmed-article:9630226 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9630226 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9630226 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9630226 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9630226 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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