1zbd
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STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A
OverviewOverview
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.
About this StructureAbout this Structure
1ZBD is a Protein complex structure of sequences from Rattus norvegicus with ZN, MG and GTP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A., Ostermeier C, Brunger AT, Cell. 1999 Feb 5;96(3):363-74. PMID:10025402
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