GTP-binding protein regulators

GTP-binding protein regulators are proteins that regulate the function of small G proteins (heterotrimeric guanine nucelotide-binding peripheral membrane proteins involved in signal transduction). These include GTPase-activating proteins (GAPs) that accelerate GTP hydrolysis, guanine nucleotide dissociation inhibitors (GDIs) that prevent GDP dissociation, and guanine nucleotide exchange factors (GEFs) that facilitate exchange of GDP for GTP.

Latest Research and Reviews

News and Comment

  • News and Views |

    Traditional approaches to covalent drug design postulate that noncovalent binding affinity (Ki) should be in the nanomolar range for the lead compound to be attractive. A study by Hansen et al. suggests that covalent K-Ras inhibitors can have weak noncovalent binding affinity yet have fast chemical reactivity (kinact), because K-Ras enhances the covalent reactivity of bound inhibitor, similarly to how enzymes activate their substrates.

    • Alexander V. Statsyuk
  • News and Views |

    Drosophila Skywalker regulates the GTPase Rab35, thereby controlling the turnover of synaptic-vesicle proteins. A new crystal structure of the TBC domain of Skywalker reveals an unexpected phosphoinositide-binding pocket, which is critical for synaptic function and is disrupted in DOORS syndrome–causing mutations in the human Skywalker homolog TBC1D24.

    • Steven J Del Signore
    •  & Avital A Rodal