SNARE Domain

Domain Binding and Function

While the mechanism by which a vesicle fuses with its proper membrane target is poorly understood, it appears to involve a highly conserved set of proteins called SNAREs (Soluble NSF Attachment protein [SNAP] Receptors). SNARE proteins are believed to mediate most, if not all, cellular membrane fusion events. Most SNAREs are C-terminally anchored integral membrane proteins capable of entering into a coiled-coil interaction with other SNARE proteins. All SNARE proteins share a homologous domain of approximately 60 amino acids referred to as the SNARE domain. The SNARE domain acts as a protein—protein interaction module in the assembly of a SNARE protein complex. While monomeric SNARE motifs are largely unstructured, they assemble into a protease resistant core complex. Interestingly, different SNARE family members are distributed on distinct membranes throughout the cell, suggesting they may play a role in targeting during vesicular transport. However, the formation of SNARE core complexes appears to be rather promiscuous with little specificity.

Structure Reference

1. Sutton, R.B. et al. (1998) Nature 395(6700), 347–353.

Examples of Domain Proteins

Binding Examples

SNARE complexes	SNARE domain proteins in complexes
Rat Synaptic Fusion SNARE Complex	Syntaxin-1A (Sx), Synaptobrevin-II (Sb), SNAP-25B
Yeast Exocytic post-Golgi SNARE Complex	Snc2, Sso1, Sec9
Rat Endosomal SNARE Complex	Syntaxin-7, Vti 1b, Syntaxin 8