Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP

Article Abstract:

The crystal structure of Cdc42H proteins of the Rho family of G proteins and the analogue GMPPNP is studied in complex with GTPase-activating protein (GAP) domain of the p50rhoGAP protein. Crystallographic models for both the G protein and the GAP domain were used to determine the Cdc42H-GMPPNP/p50rhoGAP crystal structure by molecular replacement. The structure indicates that Cdc42H proteins communicate with rhoGAP proteins primarily through certain Cdc42H regions, which in turn contact a shallow pocket in the rhoGAP lined with conservative residues.

Membrane proteins, G proteins

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Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue

Article Abstract:

Research into whether GAPs stimulate the intrinsic GTPase activity of the Ras superfamily of proteins has involved determining the structure of p50rhoGAP alone and as a complex with Cdc42Hs.GMPPNP. This made it possible to identify residues that could play a role in G-protein binding and GTPase activation. It was established that the conformational rearrangement that takes place in progression from the ground state (GMPPNP) to the transition state (GDP.A1F(super -)(sub 4)) seems to be vital for GTPase activation.

Protein binding

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