| pubmed-article:15710406 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C1426807 | lld:lifeskim |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C0205438 | lld:lifeskim |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:15710406 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15710406 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:15710406 | pubmed:dateCreated | 2005-2-15 | lld:pubmed |
| pubmed-article:15710406 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15710406 | pubmed:abstractText | The recently described Spred protein family has been implicated in the modulation of receptor tyrosine kinase signalling. We report the crystal structure of the Enabled/vasodilator-stimulated phosphoprotein homology-1 (EVH1) domain from Xenopus tropicalis Spred1, solved to 1.15 A resolution. This structure confirms that the Spred EVH1 adopts the pleckstrin-homology fold, with a similar secondary structure to Enabled. A translation of one of the peptide-binding groove beta-strands narrows this groove, whilst one end of the groove shows structural flexibility. We propose that Spred1 will bind peptides that are less proline-rich than other EVH1 domains, with conformational changes indicating an induced fit. | lld:pubmed |
| pubmed-article:15710406 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15710406 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15710406 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15710406 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15710406 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15710406 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15710406 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:15710406 | pubmed:author | pubmed-author:BlundellTom... | lld:pubmed |
| pubmed-article:15710406 | pubmed:author | pubmed-author:AmayaEnriqueE | lld:pubmed |
| pubmed-article:15710406 | pubmed:author | pubmed-author:HarmerNichola... | lld:pubmed |
| pubmed-article:15710406 | pubmed:author | pubmed-author:SivakJeremy... | lld:pubmed |
| pubmed-article:15710406 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15710406 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:15710406 | pubmed:volume | 579 | lld:pubmed |
| pubmed-article:15710406 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15710406 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15710406 | pubmed:pagination | 1161-6 | lld:pubmed |
| pubmed-article:15710406 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:meshHeading | pubmed-meshheading:15710406... | lld:pubmed |
| pubmed-article:15710406 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15710406 | pubmed:articleTitle | 1.15 A crystal structure of the X. tropicalis Spred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family. | lld:pubmed |
| pubmed-article:15710406 | pubmed:affiliation | Department of Biochemistry, 80 Tennis Court Road, Cambridge, CB2 1GA, UK. nic@cryst.bioc.cam.ac.uk | lld:pubmed |
| pubmed-article:15710406 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15710406 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:493399 | entrezgene:pubmed | pubmed-article:15710406 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15710406 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15710406 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15710406 | lld:pubmed |
