RGK family G-domain:GTP analog complex structures and nucleotide-binding properties

Yehezkel Sasson, Leehee Navon-Perry, Dan Huppert, Joel A. Hirsch

Research output: Contribution to journalArticlepeer-review

Abstract

The RGK family of small G-proteins, including Rad, Gem, Rem1, and Rem2, is inducibly expressed in various mammalian tissues and interacts with voltage-dependent calcium channels and Rho kinase. Many questions remain regarding their physiological roles and molecular mechanism. Previous crystallographic studies reported RGK G-domain:guanosine di-phosphate structures. To test whether RGK proteins undergo a nucleotide-induced conformational change, we determined the crystallographic structures of Rad:GppNHp and Rem2:GppNHp to 1.7 and 1.8 Å resolutions, respectively. Also, we characterized the nucleotide-binding properties and conformations for Gem, Rad, and several structure-based mutants using fluorescence spectroscopy. The results suggest that RGK G-proteins may not behave as Ras-like canonical nucleotide-induced molecular switches. Further, the RGK proteins have differing structures and nucleotide-binding properties, which may have implications for their varied action on effectors.

Original languageEnglish
Pages (from-to)372-389
Number of pages18
JournalJournal of Molecular Biology
Volume413
Issue number2
DOIs
StatePublished - 21 Oct 2011

Keywords

  • G-protein
  • conformational switch
  • crystallography
  • fluorescence spectroscopy

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