Structure-function studies of the G-domain from human gem, a novel small G-protein

Yarden Opatowsky, Yehezkel Sasson, Isabella Shaked, Yvona Ward, Orna Chomsky-Hecht, Yael Litvak, Zvi Selinger, Kathleen Kelly, Joel A. Hirsch*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 Å resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations.

Original languageAmerican English
Pages (from-to)5959-5964
Number of pages6
JournalFEBS Letters
Issue number25
StatePublished - 30 Oct 2006

Bibliographical note

Funding Information:
Thanks go to the staff of ID14-4 (ESRF, France) for assistance with diffraction experiments. We thank Doug Andres for generously sharing Cav β expression constructs. Preliminary studies were supported by a grant from the US–Israel Binational Science Foundation (JAH, KK). Continuing work has been funded by a grant to JAH from the Israel Cancer Research Fund and by NIH grant EY 03529 to ZS. Appendix A


  • Calcium channel
  • Crystallography
  • Cytoskeleton
  • G-protein
  • Nucleotide


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