| pubmed-article:10747019 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10747019 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:10747019 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:10747019 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:10747019 | lifeskim:mentions | umls-concept:C1518827 | lld:lifeskim |
| pubmed-article:10747019 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:10747019 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:10747019 | lifeskim:mentions | umls-concept:C1540661 | lld:lifeskim |
| pubmed-article:10747019 | lifeskim:mentions | umls-concept:C1709287 | lld:lifeskim |
| pubmed-article:10747019 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
| pubmed-article:10747019 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:10747019 | pubmed:dateCreated | 2000-5-15 | lld:pubmed |
| pubmed-article:10747019 | pubmed:abstractText | The phosphotyrosine-binding (PTB) domain of the cell fate determinant Numb is involved in the formation of multiple protein complexes in vivo and can bind a diverse array of peptide sequences in vitro. To investigate the structural basis for the promiscuous nature of this protein module, we have determined its solution structure by NMR in a complex with a peptide containing an NMSF sequence derived from the Numb-associated kinase (Nak). The Nak peptide was found to adopt a significantly different structure from that of a GPpY sequence-containing peptide previously determined. In contrast to the helical turn adopted by the GPpY peptide, the Nak peptide forms a beta-turn at the NMSF site followed by another turn near the C-terminus. The Numb PTB domain appears to recognize peptides that differ in both primary and secondary structures by engaging various amounts of the binding surface of the protein. Our results suggest a mechanism through which a single PTB domain might interact with multiple distinct target proteins to control a complex biological process such as asymmetric cell division. | lld:pubmed |
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| pubmed-article:10747019 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10747019 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10747019 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10747019 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10747019 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10747019 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10747019 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:10747019 | pubmed:author | pubmed-author:LiS CSC | lld:pubmed |
| pubmed-article:10747019 | pubmed:author | pubmed-author:PawsonTT | lld:pubmed |
| pubmed-article:10747019 | pubmed:author | pubmed-author:Forman-KayJ... | lld:pubmed |
| pubmed-article:10747019 | pubmed:author | pubmed-author:ADIA SAS | lld:pubmed |
| pubmed-article:10747019 | pubmed:author | pubmed-author:ZwahlenCC | lld:pubmed |
| pubmed-article:10747019 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10747019 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:10747019 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:10747019 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10747019 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10747019 | pubmed:pagination | 1505-15 | lld:pubmed |
| pubmed-article:10747019 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10747019 | pubmed:meshHeading | pubmed-meshheading:10747019... | lld:pubmed |
| pubmed-article:10747019 | pubmed:year | 2000 | lld:pubmed |
