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Cited by 1,055

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

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

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Fasshauer, Dirk, Sutton, R. Bryan, Brunger, Axel T., Jahn, Reinhard·1998·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.95.26.15781
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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 α-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.

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Metadata

Authors
Fasshauer, D., Sutton, R. B., Brunger, A. T., & Jahn, R.
Venue
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Published
1998-12-22
Volume
95
Issue
26
Pages
15781-15786
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.95.26.15781
OpenAlex
W2047808133
Cited by
1,055
References
1
FWCI
9.01
Type
journal article
Language
en
Open access
green

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