1ZBD
STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A
Summary for 1ZBD
Entry DOI | 10.2210/pdb1zbd/pdb |
Descriptor | RABPHILIN-3A, MAGNESIUM ION, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
Functional Keywords | g protein, effector, rabcdr, synaptic exocytosis, rab protein, rab3a, rabphilin |
Biological source | Rattus norvegicus (Norway rat) More |
Cellular location | Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P63012 Cell junction, synapse (By similarity): P47709 |
Total number of polymer chains | 2 |
Total formula weight | 39786.00 |
Authors | Ostermeier, C.,Brunger, A.T. (deposition date: 1998-11-06, release date: 1999-04-02, Last modification date: 2024-10-30) |
Primary citation | Ostermeier, C.,Brunger, A.T. Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. Cell(Cambridge,Mass.), 96:363-374, 1999 Cited by PubMed Abstract: 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. PubMed: 10025402DOI: 10.1016/S0092-8674(00)80549-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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