Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs

Nat Struct Biol. 2002 Feb;9(2):107-11. doi: 10.1038/nsb746.


SNARE proteins are crucial for intracellular membrane fusion in all eukaryotes. These proteins assemble into tight complexes that connect membranes and may induce fusion. The crystal structure of the neuronal core complex is represented by an unusually long bundle of four alpha-helices connected by 16 layers of mostly hydrophobic amino acids. Here we report the 1.9 A resolution crystal structure of an endosomal SNARE core complex containing four SNAREs: syntaxin 7, syntaxin 8, vti1b and endobrevin/VAMP-8. Despite limited sequence homology, the helix alignment and the layer structure of the endosomal complex are remarkably similar to those of the neuronal complex. However, subtle variations are evident that characterize different SNARE subfamilies. We conclude that the structure of the SNARE core complex is an evolutionarily conserved hallmark of all SNARE complexes and is intimately associated with the general role of SNAREs in membrane fusion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Endosomes / chemistry*
  • Evolution, Molecular*
  • Macromolecular Substances
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism*
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Qa-SNARE Proteins
  • R-SNARE Proteins
  • Rats
  • SNARE Proteins
  • Sequence Alignment
  • Vesicular Transport Proteins*


  • Macromolecular Substances
  • Membrane Proteins
  • Qa-SNARE Proteins
  • R-SNARE Proteins
  • SNARE Proteins
  • Vamp8 protein, mouse
  • Vamp8 protein, rat
  • Vesicular Transport Proteins

Associated data

  • PDB/1GL2