作者: Ivan Dikic , Soichi Wakatsuki , Kylie J. Walters
DOI: 10.1038/NRM2767
关键词: Ubiquitin 、 Cell biology 、 Ubiquitin binding 、 Protein structure 、 Context (language use) 、 Structure–activity relationship 、 Sequence (biology) 、 Proteins metabolism 、 Extramural 、 Biochemistry 、 Biology
摘要: Ubiquitin-binding domains (UBDs) are modular elements that bind non-covalently to the protein modifier ubiquitin. Recent atomic-level resolution structures of ubiquitin-UBD complexes have revealed some mechanisms underlie versatile functions ubiquitin in vivo. The preferences UBDs for chains specific length and linkage central these functions. These originate from multimeric interactions, whereby synergistically multiple molecules, contacts with regions link molecules into a polymer. sequence context conformational changes follow their binding also contribute signalling. new structure-based insights provide strategies controlling cellular processes by targeting interfaces.