Ras GTPase-activating protein-binding protein

spinqualitylabelsall models Human G3BP1 NTF2-like domain (cyan, green) complex with Semiliki forest virus peptide (pink), sulfate, acetate, glycerol and K+ (PDB 5fw5) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Ras GTPase-activating protein-binding protein (G3BP) is a stress-granule protein that nucletes stress-granule assembly. Stress-granules are sites of mRNA storage that form by stress conditions like viral infection . Disease G3BP1 can inhibit viral replication and can promote proliferation, invasion and methasthasis of cancer cells. Relevance Besides G3BP1 implication in cancer, it was found to be functional in neuronal development and maintainance. Hence G3BP1 may function in the progression of neurodegenerative diseases. Structural highlights G3BP1 contains an N-terminal nuclear transfer factor 2 (NTF2-like) domain, RNA recognition motif domain and Arg-Gly-rich region. The 3D structure of the complex between G3BP1 and Semliki forest virus peptide shows protein:peptide ratio of 2:1. The viral peptide sequence contains twice the tetra peptide FGDF. Each FGDF sequence interacts with one molecule of G3PB1. The viral sequence FGDF interacts with hydrophobic subset and aromatic subsides of G3PB1. G3BP 3D structures 3D structures of G3BP

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