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A strategy for modulation of enzymes in the ubiquitin system.

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TLDR
This work used massively diverse combinatorial libraries of ubiquitin variants to develop inhibitors of four deubiquitinases (DUBs) and analyzed the DUB-inhibitor complexes with crystallography to report a method to target the myriad enzymes that govern ubiquitination of protein substrates.
Abstract
The ubiquitin system regulates virtually all aspects of cellular function. We report a method to target the myriad enzymes that govern ubiquitination of protein substrates. We used massively diverse combinatorial libraries of ubiquitin variants to develop inhibitors of four deubiquitinases (DUBs) and analyzed the DUB-inhibitor complexes with crystallography. We extended the selection strategy to the ubiquitin conjugating (E2) and ubiquitin ligase (E3) enzymes and found that ubiquitin variants can also enhance enzyme activity. Last, we showed that ubiquitin variants can bind selectively to ubiquitin-binding domains. Ubiquitin variants exhibit selective function in cells and thus enable orthogonal modulation of specific enzymatic steps in the ubiquitin system.

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Drugging the undruggables: exploring the ubiquitin system for drug development.

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References
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Journal ArticleDOI

The emerging complexity of protein ubiquitination

TL;DR: The present review focuses on the emerging complexity of the ubiquitin system, and reviews what is known about individual chain types, and highlights recent advances that explain how the ubiqu itin system achieves its intrinsic specificity.
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A Dynamic Role of HAUSP in the p53-Mdm2 Pathway

TL;DR: This study provides an example of an ubiquitin ligase (MDM2) that is directly regulated by a deubiquitinase (HAUSP) and also reveals a dynamic role of HAUSP in the p53-Mdm2 pathway.
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SuperPose: a simple server for sophisticated structural superposition.

TL;DR: The SuperPose web server rapidly and robustly calculates both pairwise and multiple protein structure superpositions using a modified quaternion eigenvalue approach and yields results that are intuitively more in agreement with known biological or structural data.
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Crystal Structure of a UBP-Family Deubiquitinating Enzyme in Isolation and in Complex with Ubiquitin Aldehyde

TL;DR: In this paper, the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin aldehyde were reported, showing that the UBP deubiquitinating enzymes exhibit a conserved three-domain architecture, comprising Fingers, Palm and Thumb.
Journal ArticleDOI

Ubiquitin-binding domains

TL;DR: The covalent modification of proteins by ubiquitination is a major regulatory mechanism of protein degradation and quality control, endocytosis, vesicular trafficking, cell-cycle control, stress response, DNA repair, growth-factor signalling, transcription, gene silencing and other areas of biology.
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