Probing affinity and ubiquitin linkage selectivity of ubiquitin-binding domains using mass spectrometry.

Abstract

Non-covalent interactions between ubiquitin (Ub)-modified substrates and Ub-binding domains (UBDs) are fundamental to signal transduction by Ub receptor proteins. Poly-Ub chains, linked through isopeptide bonds between internal Lys residues and the C-terminus of Ub, can be assembled with varied topologies to mediate different cellular processes. We have… (More)
DOI: 10.1021/ja300749d

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