| pubmed-article:16407336 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16407336 | lifeskim:mentions | umls-concept:C0012634 | lld:lifeskim |
| pubmed-article:16407336 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16407336 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
| pubmed-article:16407336 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:16407336 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:16407336 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:16407336 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16407336 | pubmed:dateCreated | 2006-1-12 | lld:pubmed |
| pubmed-article:16407336 | pubmed:abstractText | Serine/arginine-rich (SR) splicing factors play an important role in constitutive and alternative splicing as well as during several steps of RNA metabolism. Despite the wealth of functional information about SR proteins accumulated to-date, structural knowledge about the members of this family is very limited. To gain a better insight into structure-function relationships of SR proteins, we performed extensive sequence analysis of SR protein family members and combined it with ordered/disordered structure predictions. We found that SR proteins have properties characteristic of intrinsically disordered (ID) proteins. The amino acid composition and sequence complexity of SR proteins were very similar to those of the disordered protein regions. More detailed analysis showed that the SR proteins, and their RS domains in particular, are enriched in the disorder-promoting residues and are depleted in the order-promoting residues as compared to the entire human proteome. Moreover, disorder predictions indicated that RS domains of SR proteins were completely unstructured. Two different classification methods, the charge-hydropathy measure and the cumulative distribution function (CDF) of the disorder scores, were in agreement with each other, and they both strongly predicted members of the SR protein family to be disordered. This study emphasizes the importance of the disordered structure for several functions of SR proteins, such as for spliceosome assembly and for interaction with multiple partners. In addition, it demonstrates the usefulness of order/disorder predictions for inferring protein structure from sequence. | lld:pubmed |
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| pubmed-article:16407336 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16407336 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16407336 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16407336 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:16407336 | pubmed:author | pubmed-author:IakouchevaLil... | lld:pubmed |
| pubmed-article:16407336 | pubmed:author | pubmed-author:HaynesChadC | lld:pubmed |
| pubmed-article:16407336 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16407336 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:16407336 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16407336 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16407336 | pubmed:pagination | 305-12 | lld:pubmed |
| pubmed-article:16407336 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16407336 | pubmed:meshHeading | pubmed-meshheading:16407336... | lld:pubmed |
| pubmed-article:16407336 | pubmed:meshHeading | pubmed-meshheading:16407336... | lld:pubmed |
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| pubmed-article:16407336 | pubmed:meshHeading | pubmed-meshheading:16407336... | lld:pubmed |
| pubmed-article:16407336 | pubmed:meshHeading | pubmed-meshheading:16407336... | lld:pubmed |
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| pubmed-article:16407336 | pubmed:meshHeading | pubmed-meshheading:16407336... | lld:pubmed |
| pubmed-article:16407336 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16407336 | pubmed:articleTitle | Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins. | lld:pubmed |
| pubmed-article:16407336 | pubmed:affiliation | The Rockefeller University, Laboratory of Statistical Genetics, 1230 York Avenue, New York, NY 10021, USA. | lld:pubmed |
| pubmed-article:16407336 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16407336 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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