| pubmed-article:9428519 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9428519 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9428519 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9428519 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:9428519 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:9428519 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9428519 | pubmed:dateCreated | 1998-2-2 | lld:pubmed |
| pubmed-article:9428519 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9428519 | pubmed:abstractText | The 14-3-3 family of proteins mediates signal transduction by binding to phosphoserine-containing proteins. Using phosphoserine-oriented peptide libraries to probe all mammalian and yeast 14-3-3s, we identified two different binding motifs, RSXpSXP and RXY/FXpSXP, present in nearly all known 14-3-3 binding proteins. The crystal structure of 14-3-3zeta complexed with the phosphoserine motif in polyoma middle-T was determined to 2.6 A resolution. The bound peptide is in an extended conformation, with a tight turn created by the pS +2 Pro in a cis conformation. Sites of peptide-protein interaction in the complex rationalize the peptide library results. Finally, we show that the 14-3-3 dimer binds tightly to single molecules containing tandem repeats of phosphoserine motifs, implicating bidentate association as a signaling mechanism with molecules such as Raf, BAD, and Cbl. | lld:pubmed |
| pubmed-article:9428519 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9428519 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9428519 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9428519 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9428519 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9428519 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:9428519 | pubmed:author | pubmed-author:CantleyL CLC | lld:pubmed |
| pubmed-article:9428519 | pubmed:author | pubmed-author:AitkenAA | lld:pubmed |
| pubmed-article:9428519 | pubmed:author | pubmed-author:CareyT ETE | lld:pubmed |
| pubmed-article:9428519 | pubmed:author | pubmed-author:RittingerKK | lld:pubmed |
| pubmed-article:9428519 | pubmed:author | pubmed-author:LeffersHH | lld:pubmed |
| pubmed-article:9428519 | pubmed:author | pubmed-author:VoliniaSS | lld:pubmed |
| pubmed-article:9428519 | pubmed:author | pubmed-author:YaffeM BMB | lld:pubmed |
| pubmed-article:9428519 | pubmed:author | pubmed-author:SmerdonS JSJ | lld:pubmed |
| pubmed-article:9428519 | pubmed:author | pubmed-author:GamblinS JSJ | lld:pubmed |
| pubmed-article:9428519 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9428519 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:9428519 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:9428519 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9428519 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9428519 | pubmed:pagination | 961-71 | lld:pubmed |
| pubmed-article:9428519 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9428519 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9428519 | pubmed:articleTitle | The structural basis for 14-3-3:phosphopeptide binding specificity. | lld:pubmed |
| pubmed-article:9428519 | pubmed:affiliation | Department of Medicine, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02215, USA. | lld:pubmed |
| pubmed-article:9428519 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9428519 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9428519 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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