The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyGraduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
2006-05-16Keywords
Animals; Drosophila Proteins; Models, Molecular; Protein Conformation; Vesicular Transport ProteinsLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
Nat Struct Mol Biol. 2006 Jun;13(6):555-6. Epub 2006 May 14. Link to article on publisher's siteDOI
10.1038/nsmb1096Permanent Link to this Item
http://hdl.handle.net/20.500.14038/32559PubMed ID
16699513Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1038/nsmb1096