Structural Basis of Rab Effector Specificity

  • Ostermeier C
  • Brunger A
Citations of this article
Mendeley users who have this article in their library.


The small G protein Rab3A plays an important role in the regulation of neurotransmitter release. The crystal structure of activated Rab3A/GTP/Mg2+bound to the effector domain of rabphilin-3A was solved to 2.6 Å resolution. Rabphilin-3A contacts Rab3A in two distinct areas. The first interface involves the Rab3A switch I and switch II regions, which are sensitive to the nucleotide-binding state of Rab3A. The second interface consists of a deep pocket in Rab3A that interacts with a SGAWFF structural element of rabphilin- 3A. Sequence and structure analysis, and biochemical data suggest that this pocket, or Rab complementarity-determining region (RabCDR), establishes a specific interaction between each Rab protein and its effectors. RabCDRs could be major determinants of effector specificity during vesicle trafficking and fusion.




Ostermeier, C., & Brunger, A. T. (1999). Structural Basis of Rab Effector Specificity. Cell, 96(3), 363–374.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free