Molecular basis for ubiquitin ligase CRL2<sup>FEM1C</sup>-mediated recognition of C-degron.

Yan, Xiaojie; Wang, Xiaolu; Li, Yao; Zhou, Mengqi; Li, Yanjun; Song, Lili; Mi, Wenyi; Min, Jinrong; Dong, Cheng

Molecular basis for ubiquitin ligase CRL2^FEM1C-mediated recognition of C-degron.

Yan, Xiaojie; Wang, Xiaolu; Li, Yao; Zhou, Mengqi; Li, Yanjun; Song, Lili; Mi, Wenyi; Min, Jinrong; Dong, Cheng.

Yan X; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, China.
Wang X; Department of Pharmacology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, China.
Li Y; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, China.
Zhou M; Structural Genomics Consortium and Department of Physiology, University of Toronto, Toronto, Ontario, Canada.
Li Y; Structural Genomics Consortium and Department of Physiology, University of Toronto, Toronto, Ontario, Canada.
Song L; Department of Immunology, Tianjin Key Laboratory of Cellular and Molecular Immunology, Key Laboratory of Diseases and Microenvironment of Ministry of Education of China, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, School of Basic Medical Sciences,
Mi W; Department of Immunology, Tianjin Key Laboratory of Cellular and Molecular Immunology, Key Laboratory of Diseases and Microenvironment of Ministry of Education of China, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, School of Basic Medical Sciences,
Min J; Structural Genomics Consortium and Department of Physiology, University of Toronto, Toronto, Ontario, Canada. jr.min@utoronto.ca.
Dong C; Department of Biochemistry and Molecular Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, China. dongcheng@tmu.edu.cn.

Nat Chem Biol ; 17(3): 263-271, 2021 03.

Article en En | MEDLINE | ID: mdl-33398170

Asunto(s)

Arginina/química; Proteínas Portadoras/química; Proteínas de Ciclo Celular/química; Complejo de la Endopetidasa Proteasomal/metabolismo; Complejos de Ubiquitina-Proteína Ligasa/química; Secuencia de Aminoácidos; Arginina/metabolismo; Sitios de Unión; Proteínas Portadoras/genética; Proteínas Portadoras/metabolismo; Proteínas de Ciclo Celular/genética; Proteínas de Ciclo Celular/metabolismo; Clonación Molecular; Cristalografía por Rayos X; Escherichia coli/genética; Escherichia coli/metabolismo; Expresión Génica; Vectores Genéticos/química; Vectores Genéticos/metabolismo; Células HEK293; Humanos; Modelos Moleculares; Unión Proteica; Conformación Proteica en Hélice alfa; Conformación Proteica en Lámina beta; Dominios y Motivos de Interacción de Proteínas; Proteolisis; Proteínas Recombinantes/química; Proteínas Recombinantes/genética; Proteínas Recombinantes/metabolismo; Alineación de Secuencia; Homología de Secuencia de Aminoácido; Especificidad por Sustrato; Complejos de Ubiquitina-Proteína Ligasa/genética; Complejos de Ubiquitina-Proteína Ligasa/metabolismo

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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Arginina / Proteínas Portadoras / Proteínas de Ciclo Celular / Complejos de Ubiquitina-Proteína Ligasa / Complejo de la Endopetidasa Proteasomal Límite: Humans Idioma: En Año: 2021 Tipo del documento: Article

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