The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel.

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第一作者： Stephanie J,Ward

第一单位： From the Centre for Biomolecular Sciences, School of Pharmacy, University of Nottingham, Nottingham NG7 2RD, United Kingdom.

作者： Stephanie J,Ward ^[1] ; Hayley E,Gratton ^[1] ; Peni,Indrayudha ^[1] ; Camille,Michavila ^[1] ; Rishov,Mukhopadhyay ^[1] ; Sigrun K,Maurer ^[1] ; Simon G,Caulton ^[1] ; Jonas,Emsley ^[1] ; Ingrid,Dreveny ^[2]

作者单位： From the Centre for Biomolecular Sciences, School of Pharmacy, University of Nottingham, Nottingham NG7 2RD, United Kingdom. ^[1] From the Centre for Biomolecular Sciences, School of Pharmacy, University of Nottingham, Nottingham NG7 2RD, United Kingdom ingrid.dreveny@nottingham.ac.uk. ^[2]

关键词 USP15 catalytic triad crystal structure cysteine protease deubiquitylation (deubiquitination)protease protein conformation protein degradation ubiquitin ubiquitin-specific protease

主题词催化域(Catalytic Domain);人类(Humans);分子动力学模拟(Molecular Dynamics Simulation);蛋白质结合(Protein Binding);序列同源性, 氨基酸(Sequence Homology, Amino Acid);泛素(Ubiquitin)

DOI 10.1074/jbc.RA118.003857

PMID 30228188

发布时间 2022-01-29

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