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Computationally designed peptide inhibitors of the ubiquitin E3 ligase SCF(Fbx4).

ABSTRACT: A structure-based computational approach was used to rationally design peptide inhibitors that can target an E3 ligase (SCF(Fbx4) )-substrate (TRF1) interface and subsequent ubiquitylation. Characterization of the inhibitors demonstrates that our sequence-optimization protocol results in an increase in peptide-TRF1 affinity without compromising peptide-protein specificity.

SUBMITTER: Lee J 

PROVIDER: S-EPMC4028150 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Computationally designed peptide inhibitors of the ubiquitin E3 ligase SCF(Fbx4).

Lee Junglim J   Sammond Deanne W DW   Fiorini Zeno Z   Saludes Jonel P JP   Resch Michael G MG   Hao Bing B   Wang Wei W   Yin Hang H   Liu Xuedong X  

Chembiochem : a European journal of chemical biology 20130211 4

A structure-based computational approach was used to rationally design peptide inhibitors that can target an E3 ligase (SCF(Fbx4) )-substrate (TRF1) interface and subsequent ubiquitylation. Characterization of the inhibitors demonstrates that our sequence-optimization protocol results in an increase in peptide-TRF1 affinity without compromising peptide-protein specificity. ...[more]

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