| pubmed-article:11031113 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11031113 | lifeskim:mentions | umls-concept:C1956036 | lld:lifeskim |
| pubmed-article:11031113 | lifeskim:mentions | umls-concept:C0900627 | lld:lifeskim |
| pubmed-article:11031113 | lifeskim:mentions | umls-concept:C1333226 | lld:lifeskim |
| pubmed-article:11031113 | lifeskim:mentions | umls-concept:C1705335 | lld:lifeskim |
| pubmed-article:11031113 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11031113 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:11031113 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:11031113 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
| pubmed-article:11031113 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11031113 | pubmed:dateCreated | 2000-11-14 | lld:pubmed |
| pubmed-article:11031113 | pubmed:abstractText | PDZ domains are modular protein units that play important roles in organizing signal transduction complexes. PDZ domains mediate interactions with both C-terminal peptide ligands and other PDZ domains. Here, we used PDZ domains from neuronal nitric oxide synthase (nNOS) and postsynaptic density protein-95 (PSD-95) to explore the mechanism for PDZ-dimer formation. The nNOS PDZ domain terminates with a approximately 30 residue amino acid beta-finger peptide that is shown to be required for nNOS/PSD-95 PDZ dimer formation. In addition, formation of the PDZ dimer requires this beta-finger peptide to be physically anchored to the main body of the canonical nNOS PDZ domain. A buried salt bridge between the beta-finger and the PDZ domain induces and stabilizes the beta-hairpin structure of the nNOS PDZ domain. In apo-nNOS, the beta-finger peptide is partially flexible and adopts a transient beta-strand like structure that is stabilized upon PDZ dimer formation. The flexibility of the NOS PDZ beta-finger is likely to play a critical role in supporting the formation of nNOS/PSD-95 complex. The experimental data also suggest that nNOS PDZ and the second PDZ domain of PSD-95 form a "head-to-tail" dimer similar to the nNOS/syntrophin complex characterized by X-ray crystallography. | lld:pubmed |
| pubmed-article:11031113 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11031113 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11031113 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11031113 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11031113 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11031113 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11031113 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11031113 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11031113 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11031113 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11031113 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:11031113 | pubmed:author | pubmed-author:TochioHH | lld:pubmed |
| pubmed-article:11031113 | pubmed:author | pubmed-author:LiuK JKJ | lld:pubmed |
| pubmed-article:11031113 | pubmed:author | pubmed-author:ZhangMM | lld:pubmed |
| pubmed-article:11031113 | pubmed:author | pubmed-author:BreenD HDH | lld:pubmed |
| pubmed-article:11031113 | pubmed:author | pubmed-author:ZhangQQ | lld:pubmed |
| pubmed-article:11031113 | pubmed:author | pubmed-author:MokY KYK | lld:pubmed |
| pubmed-article:11031113 | pubmed:copyrightInfo | Copyright 2000 Academic Press. | lld:pubmed |
| pubmed-article:11031113 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11031113 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:11031113 | pubmed:volume | 303 | lld:pubmed |
| pubmed-article:11031113 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11031113 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11031113 | pubmed:pagination | 359-70 | lld:pubmed |
| pubmed-article:11031113 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:11031113 | pubmed:meshHeading | pubmed-meshheading:11031113... | lld:pubmed |
| pubmed-article:11031113 | pubmed:meshHeading | pubmed-meshheading:11031113... | lld:pubmed |
| pubmed-article:11031113 | pubmed:meshHeading | pubmed-meshheading:11031113... | lld:pubmed |
| pubmed-article:11031113 | pubmed:meshHeading | pubmed-meshheading:11031113... | lld:pubmed |
| pubmed-article:11031113 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11031113 | pubmed:articleTitle | Formation of nNOS/PSD-95 PDZ dimer requires a preformed beta-finger structure from the nNOS PDZ domain. | lld:pubmed |
| pubmed-article:11031113 | pubmed:affiliation | Department of Biochemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, Kowloon, People's Republic of China. | lld:pubmed |
| pubmed-article:11031113 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11031113 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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