Unknown

Dataset Information

0

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


ABSTRACT: 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 A 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.

SUBMITTER: Opatowsky Y 

PROVIDER: S-EPMC1934412 | biostudies-literature | 2006 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Opatowsky Yarden Y   Sasson Yehezkel Y   Shaked Isabella I   Ward Yvona Y   Chomsky-Hecht Orna O   Litvak Yael Y   Selinger Zvi Z   Kelly Kathleen K   Hirsch Joel A JA  

FEBS letters 20061006 25


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 A 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 spatial  ...[more]

Similar Datasets

| S-EPMC4110644 | biostudies-literature
| S-EPMC2678862 | biostudies-literature
| S-EPMC3200294 | biostudies-literature
| S-EPMC2995041 | biostudies-literature
| S-EPMC3439487 | biostudies-literature
| S-EPMC31848 | biostudies-literature
| S-EPMC1138181 | biostudies-other
| S-EPMC7968664 | biostudies-literature
| S-EPMC5065005 | biostudies-literature
| S-EPMC3312748 | biostudies-literature