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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles.

The exocyst is a conserved protein complex essential for trafficking secretory vesicles to the plasma membrane. The structure of the C-terminal domain of the exocyst subunit Sec6p reveals multiple helical bundles, which are structurally and topologically similar to Exo70p and the C-terminal domains of Exo84p and Sec15, despite <10% sequence identity. The helical bundles appear to be evolutionarily related molecular scaffolds that have diverged to create functionally distinct exocyst proteins.[1]

References

  1. The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles. Sivaram, M.V., Furgason, M.L., Brewer, D.N., Munson, M. Nat. Struct. Mol. Biol. (2006) [Pubmed]
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