Structural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein
| Autor: | Maozhen Luo, Zhiwei Han, Guoye Huang, Rongfang Li, Yi Liu, Junjie Lu, Lin Liu, Rui Miao |
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| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Plant Signaling & Behavior, Vol 17, Iss 1 (2022) |
| Druh dokumentu: | article |
| ISSN: | 1559-2316 1559-2324 15592324 |
| DOI: | 10.1080/15592324.2021.2024405 |
| Popis: | 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. |
| Databáze: | Directory of Open Access Journals |
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