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• W2080347232 abstract "As a member of the dynamin superfamily human guanylate‐binding protein 1 (hGBP1) binds and hydrolyses GTP thereby undergoing structural changes which lead to self‐assembly of the protein. Here, we employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C‐terminal domain of hGBP1 and the rest of the protein are identified which report a large change of accessibility by the compound after addition of GTP. Our results indicate that nucleotide hydrolysis induces a domain movement in hGBP1, which we suggest enables further assembly of the protein." @default.
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• W2080347232 date "2009-05-20" @default.
• W2080347232 modified "2023-10-15" @default.
• W2080347232 title "Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis" @default.
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• W2080347232 doi "https://doi.org/10.1016/j.febslet.2009.05.027" @default.
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