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Three-dimensional structure of the neuronal-Sec1–syntaxin 1a complex

Author

Listed:
  • Kira M. S. Misura

    (Stanford University School of Medicine)

  • Richard H. Scheller

    (Molecular and Cellular Physiology and the Howard Hughes Medical Institute, Stanford University School of Medicine)

  • William I. Weis

    (Stanford University School of Medicine)

Abstract

Syntaxin 1a and neuronal Sec1 (nSec1) form an evolutionarily conserved heterodimer that is essential for vesicle trafficking and membrane fusion. The crystal structure of the nSec1–syntaxin 1a complex, determined at 2.6 Å resolution, reveals that major conformational rearrangements occur in syntaxin relative to both the core SNARE complex and isolated syntaxin. We identify regions of the two proteins that seem to determine the binding specificity of particular Sec1 proteins for syntaxin isoforms, which is likely to be important for the fidelity of membrane trafficking. The structure also indicates mechanisms that might couple the action of upstream effector proteins to conformational changes in syntaxin 1a and nSec1 that lead to core complex formation and membrane fusion.

Suggested Citation

  • Kira M. S. Misura & Richard H. Scheller & William I. Weis, 2000. "Three-dimensional structure of the neuronal-Sec1–syntaxin 1a complex," Nature, Nature, vol. 404(6776), pages 355-362, March.
    • Handle: RePEc:nat:nature:v:404:y:2000:i:6776:d:10.1038_35006120
    DOI: 10.1038/35006120
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    Cited by:

    1. Marieke Meijer & Miriam Öttl & Jie Yang & Aygul Subkhangulova & Avinash Kumar & Zicheng Feng & Torben W. Voorst & Alexander J. Groffen & Jan R. T. Weering & Yongli Zhang & Matthijs Verhage, 2024. "Tomosyns attenuate SNARE assembly and synaptic depression by binding to VAMP2-containing template complexes," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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