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Plos One : Distinct Ubiquitin Binding Modes Exhibited by Sh3 Domains ; Molecular Determinants and Functional Implications, Volume 8

By Buday, Laszlo

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Book Id: WPLBN0003946908
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos One : Distinct Ubiquitin Binding Modes Exhibited by Sh3 Domains ; Molecular Determinants and Functional Implications, Volume 8  
Author: Buday, Laszlo
Volume: Volume 8
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Historic
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Publisher: Plos

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Buday, L. (n.d.). Plos One : Distinct Ubiquitin Binding Modes Exhibited by Sh3 Domains ; Molecular Determinants and Functional Implications, Volume 8. Retrieved from http://netlibrary.net/


Description
Description : SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation. We have determined the structure of the complex between first CD2AP SH3 domain and ubiquitin and performed a structural and mutational analysis to decipher the determinants of the SH3-C binding mode to ubiquitin. We found that the Phe-to-Tyr mutation in CD2AP and in the homologous CIN85 SH3-C domain does not abrogate ubiquitin binding, in contrast to previous hypothesis and our findings for the first two CD2AP SH3 domains. The similar alternative binding mode of the SH3-C domains of these related adaptor proteins is characterised by a higher affinity to C-terminal extended ubiquitin molecules. We conclude that CD2AP/CIN85 SH3-C domain interaction with ubiquitin constitutes a new ubiquitin-binding mode involved in a different cellular function and thus changes the previously established mechanism of EGF-dependent CD2AP/CIN85 mono-ubiquitination.

 

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