Support for shared ancestry of GAPs

Katrin Rittinger, William R. Taylor, Stephen J. Smerdon () and Steven J. Gamblin
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Katrin Rittinger: Structural Biology Group, National Institute for Medical Research
William R. Taylor: Structural Biology Group, National Institute for Medical Research
Stephen J. Smerdon: Structural Biology Group, National Institute for Medical Research
Steven J. Gamblin: Structural Biology Group, National Institute for Medical Research

Nature, 1998, vol. 392, issue 6675, 448-448

Abstract: Abstract The Ras superfamily of monomeric GTPase proteins comprises six subfamilies, each with specific cellular functions, but all these subfamilies share a common fold and a common mechanism for hydrolysing GTP. Unlike their cognate guanine-nucleotide-binding (G) proteins, GTPase-activating proteins (GAPs) specific for the Rho or Ras subfamilies show no significant homology at the level of protein sequence. However, we have now noticed a structural similarity which suggests that, like their G proteins, these GAPs have evolved from a common ancestor.

Date: 1998
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DOI: 10.1038/33043

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