• Media type: E-Article
  • Title: Molecular Dynamics Simulations Reveal Structural Interconnections within Sec14-PH Bipartite Domain from Human Neurofibromin
  • Contributor: Rizza, Fabio; Vertemara, Jacopo; Tisi, Renata
  • Published: MDPI AG, 2022
  • Published in: International Journal of Molecular Sciences, 23 (2022) 10, Seite 5707
  • Language: English
  • DOI: 10.3390/ijms23105707
  • ISSN: 1422-0067
  • Origination:
  • Footnote:
  • Description: Neurofibromin, the main RasGAP in the nervous system, is a 2818 aa protein with several poorly characterized functional domains. Mutations in the NF1-encoding gene lead to an autosomal dominant syndrome, neurofibromatosis, with an incidence of 1 out of 3000 newborns. Missense mutations spread in the Sec14-PH-encoding sequences as well. Structural data could not highlight the defect in mutant Sec14-PH functionality. By performing molecular dynamics simulations at different temperatures, we found that the lid-lock is fundamental for the structural interdependence of the NF1 bipartite Sec14-PH domain. In fact, increased flexibility in the lid-lock loop, observed for the K1750Δ mutant, leads to disconnection of the two subdomains and can affect the stability of the Sec14 subdomain.
  • Access State: Open Access