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• W1974473906 abstract "Human guanylate binding protein 1 (hGBP1) belongs to the dynamin superfamily of large GTPases (LGs). In the course of GTP hydrolysis, the protein undergoes structural changes leading to self-assembly of the protein, which is a characteristic property of all family members. For self-assembly, the protein employs two distinct interaction sites, one of which is located within the LG domain of the protein located at the N-terminus, and the second is located in the C-terminal alpha-helical domain. Here, we identify intramolecular contacts between the LG domain and the helical part of hGBP1, which relay nucleotide-dependent structural changes from the N-terminus to the C-terminus and thereby mediate tetramer formation of the protein through a second contact site at the C-terminus. Furthermore, we demonstrate the impact of this intramolecular communication on the enzymatic activity of hGBP1 and on its cellular localization." @default.
• W1974473906 created "2016-06-24" @default.
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• W1974473906 date "2010-07-01" @default.
• W1974473906 modified "2023-09-30" @default.
• W1974473906 title "Mechanism of GTPase-Activity-Induced Self-Assembly of Human Guanylate Binding Protein 1" @default.
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• W1974473906 doi "https://doi.org/10.1016/j.jmb.2010.04.053" @default.
• W1974473906 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20450919" @default.
• W1974473906 hasPublicationYear "2010" @default.
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