da Fonseca, P. C.A. and Morris, E. P. (2015) Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core. Nature Communications, 6, 7573. (doi: 10.1038/ncomms8573) (PMID:26133119) (PMCID:PMC4506541)
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Abstract
The proteasome is a highly regulated protease complex fundamental for cell homeostasis and controlled cell cycle progression. It functions by removing a wide range of specifically tagged proteins, including key cellular regulators. Here we present the structure of the human 20S proteasome core bound to a substrate analogue inhibitor molecule, determined by electron cryo-microscopy (cryo-EM) and single-particle analysis at a resolution of around 3.5 Å. Our map allows the building of protein coordinates as well as defining the location and conformation of the inhibitor at the different active sites. These results open new prospects to tackle the proteasome functional mechanisms. Moreover, they also further demonstrate that cryo-EM is emerging as a realistic approach for general structural studies of protein–ligand interactions.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | da Fonseca, Professor Paula |
Authors: | da Fonseca, P. C.A., and Morris, E. P. |
College/School: | College of Medical Veterinary and Life Sciences > School of Molecular Biosciences |
Journal Name: | Nature Communications |
Publisher: | Nature Publishing Group |
ISSN: | 2041-1723 |
ISSN (Online): | 2041-1723 |
Copyright Holders: | Copyright © 2015 Macmillan Publishers Limited |
First Published: | First published in Nature Communications 6(1):7573 |
Publisher Policy: | Reproduced under a Creative Commons licence |
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