1ZBD

STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY: CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAB3A COMPLEXED WITH THE EFFECTOR DOMAIN OF RABPHILIN-3A

1ZBD の概要

• エントリーDOI: 10.2210/pdb1zbd/pdb
• 分子名称: RABPHILIN-3A, MAGNESIUM ION, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: g protein, effector, rabcdr, synaptic exocytosis, rab protein, rab3a, rabphilin
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P63012; Cell junction, synapse (By similarity): P47709
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39786.00

構造登録者

Ostermeier, C.,Brunger, A.T. (登録日: 1998-11-06, 公開日: 1999-04-02, 最終更新日: 2024-10-30)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.6 Å)