GoLoco motif proteins binding to Gα(i1): insights from molecular simulations

Molecular dynamics simulations, computational alanine scanning and sequence analysis were used to investigate the structural properties of the Gα(i1)/GoLoco peptide complex. Using these methodologies, binding of the GoLoco motif peptide to the Gα(i1) subunit was found to restrict the relative movement of the helical and catalytic domains in the Gα(i1) subunit, which is in agreement with a proposed mechanism of GDP dissociation inhibition by GoLoco motif proteins. In addition, the results provide further insights into the role of the “Switch IV” region located within the helical domain of Gα, the conformation of which might be important for interactions with various Gα partners. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00894-009-0516-z) contains supplementary material, which is available to authorized users.