Hemifusion in SNARE-mediated membrane fusion

SNAREs are essential for intracellular membrane fusion. Using EPR, we determined the structure of the transmembrane domain (TMD) of the vesicle (v)-SNARE Snc2p involved in trafficking in yeast. Structural features of the TMD were used to design a v-SNARE mutant in which about half of the TMD was del...

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Veröffentlicht in:	Nature structural & molecular biology 2005-05, Vol.12 (5), p.417-422
Hauptverfasser:	Shin, Yeon-Kyun, Xu, Yibin, Zhang, Fan, Su, Zengliu, McNew, James A
Format:	Artikel
Sprache:	eng
Schlagworte:	Biochemistry Biological Microscopy Biomedical and Life Sciences Electron Spin Resonance Spectroscopy Life Sciences Lipids Lipids - pharmacology Membrane Biology Membrane Fusion Membrane proteins Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Models, Molecular Molecular biology Mutants Mutation - genetics Physiological aspects Protein Structure Protein Structure, Tertiary Proteins R-SNARE Proteins Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism SNARE Proteins Spin Labels Structure Vesicular Transport Proteins - chemistry Vesicular Transport Proteins - genetics Vesicular Transport Proteins - metabolism Yeasts
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