The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with RaplA and a GTP analogue

The X-ray crystal structure of the complex between the Ras-related protein RaplA in the GTP-analogue (GppNHp) form and the Ras-binding domain (RBD) of the Ras effector molecule c-Raf1, a Ser/Thr-specific protein kinase, has been solved to a resolution of 2.2 Å. It shows that RBD has the ubiquitin superfold and that the structure of RaplA is very similar to that of Ras. The interaction between the two proteins is mediated by an apparent central antiparallel β-sheet formed by strands B1–B2 from RBD and strands β2–β3 from RaplA. Complex formation is mediated by main-chain and side-chain interactions of the so-called effector residues in the switch I region of RaplA.

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