Sandbox 208: Difference between revisions
No edit summary |
|||
| Line 20: | Line 20: | ||
Both REP and GDI are considered as Rab molecular chaperones. They have similar organization, in particular, their Rab binding interface which is well conserved. | Both REP and GDI are considered as Rab molecular chaperones. They have similar organization, in particular, their Rab binding interface which is well conserved. | ||
= Substrate binding = | =Structure= | ||
==Overall structure== | |||
== Substrate binding == | |||
Contacts between prenylated Rab proteins and GDI are established through a combination of polar and hydrophobic interactions. These interactions involve the switch I and switch II regions, the C-terminus of Rab, including the geranylgeranyl moiety and different regions of the domain I and II of GDI. Several conformational changes in the GDI molecule occur upon Rab binding. | Contacts between prenylated Rab proteins and GDI are established through a combination of polar and hydrophobic interactions. These interactions involve the switch I and switch II regions, the C-terminus of Rab, including the geranylgeranyl moiety and different regions of the domain I and II of GDI. Several conformational changes in the GDI molecule occur upon Rab binding. | ||