Your browser doesn't support javascript.
loading
Fascin - F-actin interaction studied by molecular dynamics simulation and protein network analysis.
Wu, Xiaodong; Li, Dajia; Chen, Yang; Wang, Liangdong; Xu, Li-Yan; Li, En-Min; Dong, Geng.
Afiliación
  • Wu X; Department of Biochemistry and Molecular Biology, Shantou University Medical College, Shantou, PR China.
  • Li D; Department of Biochemistry and Molecular Biology, Shantou University Medical College, Shantou, PR China.
  • Chen Y; Department of Biochemistry and Molecular Biology, Shantou University Medical College, Shantou, PR China.
  • Wang L; Department of Pathology, The First People's Hospital of Yunnan Province, Kunming, Yunnan Province, China.
  • Xu LY; Department of Biochemistry and Molecular Biology, Shantou University Medical College, Shantou, PR China.
  • Li EM; Key Laboratory of Molecular Biology in High Cancer Incidence Coastal Area of Guangdong Higher Education Institutes, Shantou University Medical College, Shantou, PR China.
  • Dong G; Cancer Research Center, Shantou University Medical College, Shantou, PR China.
J Biomol Struct Dyn ; 42(1): 435-444, 2024.
Article en En | MEDLINE | ID: mdl-37029713
Actin bundles are an important component of cellular cytoskeleton and participate in the movement of cells. The formation of actin bundles requires the participation of many actin binding proteins (ABPs). Fascin is a member of ABPs, which plays a key role in bundling filamentous actin (F-actin) to bundles. However, the detailed interactions between fascin and F-actin are unclear. In this study, we construct an atomic-level structure of fascin - F-actin complex based on a rather poor cryo-EM data with resolution of 20 nm. We first optimized the geometries of the complex by molecular dynamics (MD) simulation and analyzed the binding site and pose of fascin which bundles two F-actin chains. Next, binding free energy of fascin was calculated by MM/GBSA method. Finally, protein structure network analysis (PSNs) was performed to analyze the key residues for fascin binding. Our results show that residues of K22, E27, E29, K41, K43, R110, R149, K358, R408 and K471 on fascin are important for its bundling, which are in good agreement with the experimental data. On the other hand, the consistent results indicate that the atomic-level model of fascin - F-actin complex is reliable. In short, this model can be used to understand the detailed interactions between fascin and F-actin, and to develop novel potential drugs targeting fascin.Communicated by Ramaswamy H. Sarma.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Actinas / Simulación de Dinámica Molecular Idioma: En Revista: J Biomol Struct Dyn Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Actinas / Simulación de Dinámica Molecular Idioma: En Revista: J Biomol Struct Dyn Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido