Document Detail


Probing domain swapping for the neuronal SNARE complex with electron paramagnetic resonance.
MedLine Citation:
PMID:  11969405     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Dae-Hyuk Kweon; Yong Chen; Fan Zhang; Michelle Poirier; Chang Sup Kim; Yeon-Kyun Shin
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  41     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  2002 Apr 
Date Detail:
Created Date:  2002-04-23     Completed Date:  2002-05-29     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5449-52     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.
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MeSH Terms
Descriptor/Qualifier:
Cyclic N-Oxides / 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:
GM51290/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
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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