Issue 2, 2012
From the journal:

Chemical Communications

Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding†

Nadine D. Weikart,a   Stefanie Sommera  and  Henning D. Mootz*a  

* Corresponding authors

a Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Str. 2, D-48149 Münster, Germany
E-mail: henning.mootz@uni-muenster.de

Abstract

A new route to the synthesis of triazole-linked ubiquitin dimers (diUbs) as structural analogs of the seven diUbs is reported. Binding studies with the Lys48-specific UBA domain of the Mud1 protein suggest that they represent functionally suitable surrogates of their native counterparts linked by an isopeptide bond.

Graphical abstract: Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C1CC15834A
Article type
Communication
Submitted
20 Sep 2011
Accepted
26 Oct 2011
First published
18 Nov 2011

Chem. Commun., 2012,48, 296-298

Permissions

Request permissions

Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding

N. D. Weikart, S. Sommer and H. D. Mootz, Chem. Commun., 2012, 48, 296 DOI: 10.1039/C1CC15834A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements