| First Author | Ostermeier C | Year | 1999 |
| Journal | Cell | Volume | 96 |
| Issue | 3 | Pages | 363-74 |
| PubMed ID | 10025402 | Mgi Jnum | J:52577 |
| Mgi Id | MGI:1329777 | Doi | 10.1016/s0092-8674(00)80549-8 |
| Citation | Ostermeier C, et al. (1999) Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. Cell 96(3):363-74 |
| abstractText | 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 A 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. |
