| pubmed-article:8757138 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8757138 | lifeskim:mentions | umls-concept:C1180347 | lld:lifeskim |
| pubmed-article:8757138 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:8757138 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8757138 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8757138 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8757138 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8757138 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8757138 | pubmed:issue | 6592 | lld:pubmed |
| pubmed-article:8757138 | pubmed:dateCreated | 1996-9-18 | lld:pubmed |
| pubmed-article:8757138 | pubmed:abstractText | The WW domain is a new protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. It is present in a number of signalling and regulatory proteins, often in several copies. Here we investigate the solution structure of the WW domain of human YAP65 (for Yes kinase-associated protein) in complex with proline-rich peptides containing the core motif PPxY. The structure of the domain with the bound peptide GTPPPPYTVG is a slightly curved, three-stranded, antiparallel beta-sheet. Two prolines pack against the first tryptophan, forming a hydrophobic buckle on the convex side of the sheet. The concave side has three exposed hydrophobic residues (tyrosine, tryptophan and leucine) which form the binding site for the ligand. A non-conserved isoleucine in the amino-terminal flanking region covers a hydrophobic patch and stabilizes the WW domain of human YAP65 in vitro. The structure of the WW domain differs from that of the SH3 domain and reveals a new design for a protein module that uses stacked aromatic surface residues to arrange a binding site for proline-rich peptides. | lld:pubmed |
| pubmed-article:8757138 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8757138 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8757138 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8757138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8757138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8757138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8757138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8757138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8757138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8757138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8757138 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8757138 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8757138 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:8757138 | pubmed:author | pubmed-author:SchultzJJ | lld:pubmed |
| pubmed-article:8757138 | pubmed:author | pubmed-author:SarasteMM | lld:pubmed |
| pubmed-article:8757138 | pubmed:author | pubmed-author:SudolMM | lld:pubmed |
| pubmed-article:8757138 | pubmed:author | pubmed-author:BaraldiEE | lld:pubmed |
| pubmed-article:8757138 | pubmed:author | pubmed-author:OschkinatHH | lld:pubmed |
| pubmed-article:8757138 | pubmed:author | pubmed-author:HyvönenMM | lld:pubmed |
| pubmed-article:8757138 | pubmed:author | pubmed-author:MaciasM JMJ | lld:pubmed |
| pubmed-article:8757138 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8757138 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8757138 | pubmed:volume | 382 | lld:pubmed |
| pubmed-article:8757138 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8757138 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8757138 | pubmed:pagination | 646-9 | lld:pubmed |
| pubmed-article:8757138 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:8757138 | pubmed:meshHeading | pubmed-meshheading:8757138-... | lld:pubmed |
| pubmed-article:8757138 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8757138 | pubmed:articleTitle | Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. | lld:pubmed |
| pubmed-article:8757138 | pubmed:affiliation | European Molecular Biology Laboratory, Heidelberg, Germany. | lld:pubmed |
| pubmed-article:8757138 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8757138 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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