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The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue.

Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A
Nature 375 554-60 (1995)
Cited: 405 times
EuropePMC logo PMID: 7791872

Abstract

The X-ray crystal structure of the complex between the Ras-related protein Rap1A 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 A. It shows that RBD has the ubiquitin superfold and that the structure of Rap1A is very similar to that of Ras. The interaction between the two proteins is mediated by an apparent central antiparallel beta-sheet formed by strands B1-B2 from RBD and strands beta 2-beta 3 from Rap1A. Complex formation is mediated by main-chain and side-chain interactions of the so-called effector residues in the switch I region of Rap1A.

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  2. Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B.. Rehmann H, Arias-Palomo E, Hadders MA, Schwede F, Llorca O, Bos JL Nature 455 124-7 (2008)

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