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J Mol Biol. 2011 Oct 21;413(2):372-89. doi: 10.1016/j.jmb.2011.08.017. Epub 2011 Aug 29.

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

Author information

1
Department of Biochemistry, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel.

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.

PMID:
21903096
DOI:
10.1016/j.jmb.2011.08.017
[Indexed for MEDLINE]

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