泛素 E3 连接酶机制的新见解。
New insights into ubiquitin E3 ligase mechanism.
机构信息
Department of Chemistry and Biochemistry, James Madison University, Harrisonburg, Virginia, USA.
1] Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. [2] Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
出版信息
Nat Struct Mol Biol. 2014 Apr;21(4):301-7. doi: 10.1038/nsmb.2780.
E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct classes of E3 ligases have been identified that stimulate transfer of ubiquitin and ubiquitin-like proteins through either a direct or an indirect mechanism. Only recently have the catalytic mechanisms of E3 ligases begun to be elucidated.
E3 连接酶完成泛素化级联反应的最后一步，催化泛素从 E2 酶转移到与底物赖氨酸形成共价键。已经鉴定出三种不同类别的 E3 连接酶，它们通过直接或间接机制刺激泛素和泛素样蛋白的转移。直到最近，E3 连接酶的催化机制才开始被阐明。
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