| Probing domain swapping for the neuronal SNARE complex with electron paramagnetic resonance. | |
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MedLine Citation:
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PMID: 11969405 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Highly conserved soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) proteins control membrane fusion at synapses. The target plasma membrane-associated SNARE proteins and the vesicle-associated SNARE protein assemble into a parallel four-helix bundle. Using a novel EPR approach, it is found that the SNARE four-helix bundles are interconnected via domain swapping that is achieved by substituting one of the two SNAP-25 helices with the identical helix from the second four-helical bundle. Domain swapping is likely to play a role in the multimerization of the SNARE complex that is required for successful membrane fusion. The new EPR application employed here should be useful to study other polymerizing proteins. |
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Authors:
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Dae-Hyuk Kweon; Yong Chen; Fan Zhang; Michelle Poirier; Chang Sup Kim; Yeon-Kyun Shin |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Biochemistry Volume: 41 ISSN: 0006-2960 ISO Abbreviation: Biochemistry Publication Date: 2002 Apr |
Date Detail:
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Created Date: 2002-04-23 Completed Date: 2002-05-29 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: United States |
Other Details:
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Languages: eng Pagination: 5449-52 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cyclic N-Oxides
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chemistry Dimerization Electron Spin Resonance Spectroscopy / methods Fourier Analysis Membrane Fusion / genetics Membrane Proteins / chemistry*, genetics, metabolism Mutagenesis, Site-Directed Nerve Tissue Proteins / chemistry*, genetics, metabolism Polymers / chemistry, metabolism Protein Structure, Secondary / genetics Protein Structure, Tertiary / genetics Recombinant Fusion Proteins / chemistry, metabolism SNARE Proteins Spin Labels Synaptosomal-Associated Protein 25 Vesicular Transport Proteins* |
| Grant Support | |
ID/Acronym/Agency:
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GM51290/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cyclic N-Oxides; 0/Membrane Proteins; 0/Nerve Tissue Proteins; 0/Polymers; 0/Recombinant Fusion Proteins; 0/SNARE Proteins; 0/Spin Labels; 0/Synaptosomal-Associated Protein 25; 0/Vesicular Transport Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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