Sandbox 208: Difference between revisions

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Both geranylgeranyl (GG) moities are located in the lipid binding site on top of each other. In this arrangement, the first bent lipid (GG1) protrudes into the core of domain II, anchoring to the lipid binding site thanks to the GDI residues <scene name='Sandbox_208/Gg1/1'>Val127, Pro128, Ala129, Ala134, Leu139, Met140, Met148, Leu152, Phe192, Met197, Cys221, Val224 and Ala225</scene>.
Both geranylgeranyl (GG) moities are located in the lipid binding site on top of each other. In this arrangement, the first bent lipid (GG1) protrudes into the core of domain II, anchoring to the lipid binding site thanks to the GDI residues <scene name='Sandbox_208/Gg1/1'>Val127, Pro128, Ala129, Ala134, Leu139, Met140, Met148, Leu152, Phe192, Met197, Cys221, Val224 and Ala225</scene>.


The second geranylgeranyl group (GG2) is located on the surface and it is aligned between helices D and E. Its binding site involves only seven hydrophobic amino acids: Met148, Leu152, Ile155, Ile193, Trp200, Tyr205 and Leu218. GG2 forms a lid shielding a large part of the buried GG1 from the solvent. The environnement of GG2 is more hydrophilic than of the buried lipid.
The second geranylgeranyl group (GG2) is located on the surface and it is aligned between helices D and E. Its binding site involves only seven hydrophobic amino acids: <scene name='Sandbox_208/Gg2/1'>Met148, Leu152, Ile155, Ile193, Trp200, Tyr205 and Leu218</scene>. GG2 forms a lid shielding a large part of the buried GG1 from the solvent. The environnement of GG2 is more hydrophilic than of the buried lipid.


GDIs have functional specificity for a particular Rab. Both yeast and mammalians GDIs contains specific residues that contribute to the strength of their interaction with distinct Rab species.
GDIs have functional specificity for a particular Rab. Both yeast and mammalians GDIs contains specific residues that contribute to the strength of their interaction with distinct Rab species.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Charlotte Simonin, Lucie Maubert