| pubmed-article:17693144 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17693144 | lifeskim:mentions | umls-concept:C0004038 | lld:lifeskim |
| pubmed-article:17693144 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:17693144 | lifeskim:mentions | umls-concept:C1184482 | lld:lifeskim |
| pubmed-article:17693144 | lifeskim:mentions | umls-concept:C1418582 | lld:lifeskim |
| pubmed-article:17693144 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:17693144 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:17693144 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:17693144 | pubmed:dateCreated | 2007-9-7 | lld:pubmed |
| pubmed-article:17693144 | pubmed:abstractText | Binding of the Cdc25c-T48 ligand to PinA from Aspergillus nidulans has been characterised by the identification of 15N and 1H resonances from 1H-15N HSQC NMR titration experiments using previous backbone assignments. It is shown that the binding site for the Cdc25c-T48 ligand with PinA is the same as in the mammalian protein Pin1, although with a reduced binding affinity. It had previously been proposed that the arginine residue (R17) in the loop I region of the Pin1 WW domain is essential for binding to the pSer/pThr-Pro motifs of phosphorylated ligands such as Cdc25c. In PinA, a fungal homologue of Pin1, the arginine residue (R17) is replaced with an asparagine residue (N17). The effect of substitution of R17 by N17 in Pin1 has been investigated via a computational study, which predicted that changing R17 to N17 in Pin1 lowers the ligand binding affinity as a result of reduced hydrogen bonding between the protein and the phosphate group of the ligand. | lld:pubmed |
| pubmed-article:17693144 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17693144 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17693144 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17693144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17693144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17693144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17693144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17693144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17693144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17693144 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17693144 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:17693144 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:17693144 | pubmed:author | pubmed-author:KatoYusukeY | lld:pubmed |
| pubmed-article:17693144 | pubmed:author | pubmed-author:TanokuraMasar... | lld:pubmed |
| pubmed-article:17693144 | pubmed:author | pubmed-author:BrownleeRober... | lld:pubmed |
| pubmed-article:17693144 | pubmed:author | pubmed-author:NgChai AnnCA | lld:pubmed |
| pubmed-article:17693144 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17693144 | pubmed:volume | 1774 | lld:pubmed |
| pubmed-article:17693144 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17693144 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17693144 | pubmed:pagination | 1208-12 | lld:pubmed |
| pubmed-article:17693144 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:meshHeading | pubmed-meshheading:17693144... | lld:pubmed |
| pubmed-article:17693144 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17693144 | pubmed:articleTitle | PinA from Aspergillus nidulans binds to pS/pT-P motifs using the same Loop I and XP groove as mammalian Pin1. | lld:pubmed |
| pubmed-article:17693144 | pubmed:affiliation | Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraqi 305-8566, Japan. | lld:pubmed |
| pubmed-article:17693144 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17693144 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17693144 | lld:entrezgene |
