Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs.

ABSTRACT: 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

SUBMITTER: Fasshauer D 

PROVIDER: S-EPMC28121 | biostudies-literature | 1998 Dec

REPOSITORIES: biostudies-literature