期刊
FEBS LETTERS
卷 583, 期 12, 页码 1923-1927出版社
WILEY
DOI: 10.1016/j.febslet.2009.05.027
关键词
Ellman's reagent; DTNB; Accessible surface area; Protein domain
资金
- Deutsche Forschungsgemeinschaft (DFG)
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. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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