Expression, Purification, and Preliminary X-Ray Crystallographic Analysis of the Complex of Gαi3-RGS5 from Human with GDP/Mg2+/AlF4 -
Abstract:Regulator of G-protein signaling 5 (RGS5), an inhibitor of Gq and Gi activation, is a member of the small RGS protein subfamily. However, despite significant process in the investigation of RGS5, no structure is yet available. In order to elucidate the mechanism of the RGS5 in G protein signaling pathway, we have overexpressed the RGS5 and G_i3 from human in Escherichia coli and crystallized the complex of RGS5 and Gαi3 proteins with GDP/Mg2+/AlF4 - at 3.0 Å resolution using a synchrotron radiation source. The complex crystals belong to the tetragonal space group P41212 or P43212, with unit cell parameters a=b=95.9 Å, and c=138.8 Å. Assuming one complex protein in the crystallographic asymmetric unit, the calculated Matthews parameter (VM) is 2.57 Å3/Da and solvent content is 52.2 %.
Document Type: Research Article
Affiliations: Life Sciences Division, Biomedical Research Center, Korea Institute of Science and Technology; and bCollege of Life Sciences and Biotechnology, Division of Biotechnology, Korea University, Seoul 136-701, South Korea.
Publication date: 2006-09-01
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.