Source:http://linkedlifedata.com/resource/pubmed/id/11031113
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2000-11-14
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| 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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/postsynaptic density proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0022-2836
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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| pubmed:issnType |
Print
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| pubmed:day |
27
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| pubmed:volume |
303
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
359-70
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:11031113-Amino Acid Motifs,
pubmed-meshheading:11031113-Amino Acid Sequence,
pubmed-meshheading:11031113-Binding Sites,
pubmed-meshheading:11031113-Circular Dichroism,
pubmed-meshheading:11031113-Dimerization,
pubmed-meshheading:11031113-Models, Molecular,
pubmed-meshheading:11031113-Molecular Sequence Data,
pubmed-meshheading:11031113-Mutation,
pubmed-meshheading:11031113-Nerve Tissue Proteins,
pubmed-meshheading:11031113-Nitric Oxide Synthase,
pubmed-meshheading:11031113-Nitric Oxide Synthase Type I,
pubmed-meshheading:11031113-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:11031113-Pliability,
pubmed-meshheading:11031113-Protein Binding,
pubmed-meshheading:11031113-Protein Structure, Secondary,
pubmed-meshheading:11031113-Protein Structure, Tertiary,
pubmed-meshheading:11031113-Recombinant Proteins,
pubmed-meshheading:11031113-Static Electricity,
pubmed-meshheading:11031113-Substrate Specificity,
pubmed-meshheading:11031113-Surface Plasmon Resonance
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| pubmed:year |
2000
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| pubmed:articleTitle |
Formation of nNOS/PSD-95 PDZ dimer requires a preformed beta-finger structure from the nNOS PDZ domain.
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| pubmed:affiliation |
Department of Biochemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, Kowloon, People's Republic of China.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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