Structural highlights
Publication Abstract from PubMed
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 2.5A 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. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: CSN6 and CSN6bind by x-ray crystallography (View interaction) CSN6 and CSN6bind by x ray scattering (View interaction).
The crystal structure of the MPN domain from the COP9 signalosome subunit CSN6.,Zhang H, Gao ZQ, Wang WJ, Liu GF, Shtykova EV, Xu JH, Li LF, Su XD, Dong YH FEBS Lett. 2012 Apr 24;586(8):1147-53. Epub 2012 Mar 23. PMID:22575649[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang H, Gao ZQ, Wang WJ, Liu GF, Shtykova EV, Xu JH, Li LF, Su XD, Dong YH. The crystal structure of the MPN domain from the COP9 signalosome subunit CSN6. FEBS Lett. 2012 Apr 24;586(8):1147-53. Epub 2012 Mar 23. PMID:22575649 doi:10.1016/j.febslet.2012.03.029
