Solution structure of the SGTA dimerisation domain and investigation of its interactions with the ubiquitin-like domains of BAG6 and UBL4A.

Solution structure of the SGTA dimerisation domain and investigation of its interactions with the ubiquitin-like domains of BAG6 and UBL4A.

The BAG6 complex resides in the cytosol and acts as a sorting point to target diverse hydrophobic protein substrates along their appropriate paths, including proteasomal degradation and ER membrane insertion. Composed of a trimeric complex of BAG6, TRC35 and UBL4A, the BAG6 complex is closely associ...

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Bibliographic Details
Main Authors: John F Darby, Ewelina M Krysztofinska, Peter J Simpson, Aline C Simon, Pawel Leznicki, Newran Sriskandarajah, David S Bishop, Lisa R Hale, Caterina Alfano, Maria R Conte, Santiago Martínez-Lumbreras, Arjun Thapaliya, Stephen High, Rivka L Isaacson
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4240585?pdf=render

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http://europepmc.org/articles/PMC4240585?pdf=render

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