Homo- and heterodimerization of synapsins.

@article{Hosaka1999HomoAH,
  title={Homo- and heterodimerization of synapsins.},
  author={Masahiro Hosaka and Thomas C S{\"u}dhof},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 24},
  pages={16747-53}
}
In vertebrates, synapsins constitute a family of synaptic vesicle proteins encoded by three genes. Synapsins contain a central ATP-binding domain, the C-domain, that is highly homologous between synapsins and evolutionarily conserved in invertebrates. The crystal structure of the C-domain from synapsin I revealed that it constitutes a large (>300 amino acids), independently folded domain that forms a tight dimer with or without bound ATP. We now show that the C-domains of all synapsins form… CONTINUE READING

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