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

  title={The 2.2 {\AA} crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with RaplA and a GTP analogue},
  author={Nicolas N. Nassar and Gudrun Horn and Christian Herrmann and Anna Scherer and Frank McCormick and Alfred Wittinghofer},
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… 

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