Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 DOI10.2210/pdb1zbd/pdb
DescriptorRABPHILIN-3A, MAGNESIUM ION, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
Functional Keywordsg protein, effector, rabcdr, synaptic exocytosis, rab protein, rab3a, rabphilin
Biological sourceRattus norvegicus (Norway rat)
More
Cellular locationCell membrane; Lipid-anchor; Cytoplasmic side (Potential): P63012
Cell junction, synapse (By similarity): P47709
Total number of polymer chains2
Total formula weight39786.00
Authors
Ostermeier, C.,Brunger, A.T. (deposition date: 1998-11-06, release date: 1999-04-02, Last modification date: 2024-10-30)
Primary citationOstermeier, 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: 10025402
DOI: 10.1016/S0092-8674(00)80549-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

242842

数据于2025-10-08公开中

PDB statisticsPDBj update infoContact PDBjnumon