Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 6, Pages 555-556Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1096
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Funding
- NIGMS NIH HHS [GM068803] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM068803] Funding Source: NIH RePORTER
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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.
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