{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["17(1)"],"submitter":["Luo M"],"funding":["funding"],"pubmed_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 <i>Rattus norvegicus</i> 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 si"],"journal":["Plant signaling & behavior"],"pagination":["2024405"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8959515"],"repository":["biostudies-literature"],"pubmed_title":["Structural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein."],"pmcid":["PMC8959515"],"pubmed_authors":["Liu Y","Liu L","Luo M","Huang G","Miao R","Lu J","Han Z","Li R"],"additional_accession":[]},"is_claimable":false,"name":"Structural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein.","description":"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 <i>Rattus norvegicus</i> 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 si","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-05T00:39:56.011Z","creation":"2024-11-13T22:34:17.73Z"},"accession":"S-EPMC8959515","cross_references":{"pubmed":["35135414"],"doi":["10.1080/15592324.2021.2024405"]}}