Document Detail

Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs.
MedLine Citation:
PMID:  9861047     Owner:  NLM     Status:  MEDLINE    
SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] proteins are essential for membrane fusion and are conserved from yeast to humans. Sequence alignments of the most conserved regions were mapped onto the recently solved crystal structure of the heterotrimeric synaptic fusion complex. The association of the four alpha-helices in the synaptic fusion complex structure produces highly conserved layers of interacting amino acid side chains in the center of the four-helix bundle. Mutations in these layers reduce complex stability and cause defects in membrane traffic even in distantly related SNAREs. When syntaxin-4 is modeled into the synaptic fusion complex as a replacement of syntaxin-1A, no major steric clashes arise and the most variable amino acids localize to the outer surface of the complex. We conclude that the main structural features of the neuronal complex are highly conserved during evolution. On the basis of these features we have reclassified SNARE proteins into Q-SNAREs and R-SNAREs, and we propose that fusion-competent SNARE complexes generally consist of four-helix bundles composed of three Q-SNAREs and one R-SNARE.
D Fasshauer; R B Sutton; A T Brunger; R Jahn
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  95     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1998 Dec 
Date Detail:
Created Date:  1999-01-28     Completed Date:  1999-01-28     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  15781-6     Citation Subset:  IM    
Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.
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MeSH Terms
Amino Acid Sequence
Conserved Sequence
Macromolecular Substances
Membrane Fusion
Membrane Proteins / chemistry*,  classification*
Models, Molecular
Molecular Sequence Data
Nerve Tissue Proteins / chemistry*,  classification*
Protein Structure, Secondary*
SNARE Proteins
Sequence Alignment
Sequence Homology, Amino Acid
Synapses / physiology*
Syntaxin 1
Vesicular Transport Proteins*
Reg. No./Substance:
0/Macromolecular Substances; 0/Membrane Proteins; 0/Nerve Tissue Proteins; 0/SNARE Proteins; 0/STX1A protein, human; 0/Syntaxin 1; 0/Vesicular Transport Proteins

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