Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/106985
Title: Crystal structure of Gib2, a signal-transducing protein scaffold associated with ribosomes in cryptococcus neoformans
Authors: Ero, Rya
Dimitrova, Valya Tenusheva
Chen, Yun
Bu, Wenting
Feng, Shu
Liu, Tongbao
Wang, Ping
Xue, Chaoyang
Tan, Suet Mien
Gao, Yong-Gui
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2015
Source: Ero, R., Dimitrova, V. T., Chen, Y., Bu, W., Feng, S., Liu, T., et al. (2015). Crystal structure of Gib2, a signal-transducing protein scaffold associated with ribosomes in cryptococcus neoformans. Scientific reports, 5, 8688-.
Series/Report no.: Scientific reports
Abstract: The atypical Gβ-like/RACK1 Gib2 protein promotes cAMP signalling that plays a central role in regulating the virulence of Cryptococcus neoformans. Gib2 contains a seven-bladed β transducin structure and is emerging as a scaffold protein interconnecting signalling pathways through interactions with various protein partners. Here, we present the crystal structure of Gib2 at a 2.2-Å resolution. The structure allows us to analyse the association between Gib2 and the ribosome, as well as to identify the Gib2 amino acid residues involved in ribosome binding. Our studies not only suggest that Gib2 has a role in protein translation but also present Gib2 as a physical link at the crossroads of various regulatory pathways important for the growth and virulence of C. neoformans.
URI: https://hdl.handle.net/10356/106985
http://hdl.handle.net/10220/25268
ISSN: 2045-2322
DOI: 10.1038/srep08688
Schools: School of Biological Sciences 
Rights: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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