Rep15 interacts with several rab gtpases and has a distinct fold for a rab effector

HIGHLIGHTS

• who: Amrita Rai from the Max Planck Institute of Molecular Physiology, Dortmund, GermanyLuther University have published the research: Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector, in the Journal: NATURE COMMUNICATIONS NATURE COMMUNICATIONS of 30/06/2022
• what: Taken together, the authors propose that the tyrosine residue of the RabSF3 motif (RYRTIT) provides specificity in the case of Rab3 paralogs and Rab15. The authors report the first Rep15 structure in a complex with Rab3B/C. Further, the mutagenesis experiments shed light on the origins of Rep15 selectivity towards . . .
  

   

  

  If you want to have access to all the content you need to log in!

  Thanks :)

  Username or Email

  Password

  Remember me

  Lost your password?

  If you don't have an account, you can create one here.