The crystal structure of the MPN domain from the COP9 signalosome subunit CSN6

FEBS Letters
Heng ZhangYu-Hui Dong

Abstract

The COP9 signalosome (CSN) is a multiprotein complex containing eight subunits and is highly conserved from fungi to human. CSN is proposed to widely participate in many physiological processes, including protein degradation, DNA damage response and signal transduction. Among those subunits, only CSN5 and CSN6 belong to JAMM family. CSN5 possesses isopeptidase activity, but CSN6 lacks this ability. Here we report the 2.5Å crystal structure of MPN domain from Drosophila melanogaster CSN6. Structural comparison with other MPN domains, along with bioinformation analysis, suggests that MPN domain from CSN6 may serve as a scaffold instead of a metalloprotease.

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Citations

Jan 29, 2013·Cellular and Molecular Life Sciences : CMLS·Roberta MarchioneJean-Luc Lenormand
Jan 5, 2013·Proceedings of the National Academy of Sciences of the United States of America·Aude EchalierChristian Dumas
Jul 3, 2013·Proceedings of the National Academy of Sciences of the United States of America·Jung-Hoon LeeHao Wu
Feb 12, 2014·Proceedings of the National Academy of Sciences of the United States of America·Ganesh Ramnath PathareWolfgang Baumeister
Sep 23, 2014·Biochemical and Biophysical Research Communications·Xiao-li MaTao Jiang
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Jul 22, 2014·Nature·Gondichatnahalli M LingarajuNicolas H Thomä
Apr 10, 2019·Anti-cancer Agents in Medicinal Chemistry·Zun MaoDong-Sheng Pei
Jul 4, 2012·FEBS Letters·Heng ZhangYu-Hui Dong
Mar 10, 2016·Acta Crystallographica. Section D, Structural Biology·Richard D Bunker

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