Multimedia
Movements of Gαq.
Tesmer, V. M. Science, 2005. Abstract | Full Text
Deactivation of Gα12/13 subunits
Kreutz, B. Biochemistry, 2006. Abstract | Full Text
Play [22 megabytes] |
The structures of activated Gα12 and inactivated Gα13 revealed the conformational changes that occur within this subfamily upon GTP hydrolysis. The switch regions are shown in red. The α-helical domain rotates away from the ras-like domain. Following GTP hydrolysis, the two domains of Gαi/13 are more "open" than in previously solved Gα subunits. Furthmore, the guanine nucleotide has less solvent exposed surface in the deactivated structure, hinting at the reason for slow nucleotide exchange in the 12/13 subfamily. |