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Updated: Oct 4, 2025

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
Published on: October 8, 2015
Structural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein
Maozhen Luo1, Zhiwei Han2, Guoye Huang1
1College of Agriculture, Fujian Agriculture and Forestry University, Fuzhou, China.
Abstract:
Guanine nucleotide-binding (G) proteins, namely, phosphate-binding (P) loop GTPases, play a critical role in life processes among different species. Based on the structural characteristics, G proteins can be divided into heterotrimeric G proteins, small G proteins and multiple unique unconventional G proteins. The highly conserved unconventional G protein YchF is composed of a core G domain, an inserted coiled-coil domain, and a TGS domain from the N-terminus to the C-terminus. In this review, we compared the structural characteristics of the G domain in rice OsYchF1 with those of Rattus norvegicus heterotrimeric G protein α-subunit and human small G protein Ras-related G protein C and analyzed the binding modes of these G proteins with GTP or ATP by performing molecular dynamics simulations. In summary, it will provide new insights into the enormous diversity of biological function of G proteins.
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