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Molecular dynamic simulations identifying the mechanism of holoenzyme formation by O-GlcNAc transferase and active p38α.
Wang, Yu; Zhang, Zhiyang; Liu, Xiaoyuan; Chen, Nianhang; Zhao, Yuan; Wang, Chaojie.
Afiliación
  • Wang Y; The Key Laboratory of Natural Medicine and Immuno-Engineering, Henan University, Kaifeng, 475004, China. zhaoyuan@henu.edu.cn.
  • Zhang Z; The Key Laboratory of Natural Medicine and Immuno-Engineering, Henan University, Kaifeng, 475004, China. zhaoyuan@henu.edu.cn.
  • Liu X; The Key Laboratory of Natural Medicine and Immuno-Engineering, Henan University, Kaifeng, 475004, China. zhaoyuan@henu.edu.cn.
  • Chen N; School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou, 510006, China.
  • Zhao Y; The Key Laboratory of Natural Medicine and Immuno-Engineering, Henan University, Kaifeng, 475004, China. zhaoyuan@henu.edu.cn.
  • Wang C; The Key Laboratory of Natural Medicine and Immuno-Engineering, Henan University, Kaifeng, 475004, China. zhaoyuan@henu.edu.cn.
Phys Chem Chem Phys ; 25(11): 8090-8102, 2023 Mar 15.
Article en En | MEDLINE | ID: mdl-36876722
ABSTRACT
O-N-Acetylglucosamine transferase (OGT) can catalyze the O-GlcNAc modification of thousands of proteins. The holoenzyme formation of OGT and adaptor protein is the precondition for further recognition and glycosylation of the target protein, while the corresponding mechanism is still open. Here, static and dynamic schemes based on statistics can successfully screen the feasible identifying, approaching, and binding mechanism of OGT and its typical adaptor protein p38α. The most favorable interface, energy contribution of hotspots, and conformational changes of fragments were discovered. The hydrogen bond interactions were verified as the main driving force for the whole process. The distinct characteristic of active and inactive p38α is explored and demonstrates that the phosphorylated tyrosine and threonine will form strong ion-pair interactions with Lys714, playing a key role in the dynamic identification stage. Multiple method combinations from different points of view may be helpful for exploring other systems of the protein-protein interactions.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: N-Acetilglucosaminiltransferasas / Simulación de Dinámica Molecular Tipo de estudio: Prognostic_studies Idioma: En Revista: Phys Chem Chem Phys Asunto de la revista: BIOFISICA / QUIMICA Año: 2023 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: N-Acetilglucosaminiltransferasas / Simulación de Dinámica Molecular Tipo de estudio: Prognostic_studies Idioma: En Revista: Phys Chem Chem Phys Asunto de la revista: BIOFISICA / QUIMICA Año: 2023 Tipo del documento: Article País de afiliación: China