Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
Article Abstract:
It has been possible to determine the three-dimensional structure of the complex between the proteins neuronal Sec1 (nSec1) and syntaxin 1a. The structure shows significant conformational rearrangements of syntaxin 1a in relation to the conformations seen in the core SNARE complex and in isolation. This highlights regions of the nSec1 and syntaxin 1 proteins that are likely to influence the specificity between particular isoforms of the two proteins. Syntaxin- and VAMP-like proteins associate promiscuously into SNARE complexes in vitro, and it is therefore unlikely that syntaxin-VAMP pairing in the SNARE core complex is the only determinant of vesicle targeting specificity.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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The specifics of membrane fusion
Article Abstract:
Issues are presented concerning the ability of eukaryotic cells to maintain distinct groups of proteins in a varied set of intracellular compartments. The movement of substances across cell membranes is discussed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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SNARE the rod, coil the complex
Article Abstract:
Sutton and colleagues and Poirier and colleagues have moved towards understanding the function of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), by determining important structures in forming the core fusion complexes. They have determined the orientation of the heptad-containing portions in SNAP-25, and the crystal structure of a key synaptic fusion complex has been solved.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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