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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Vöpel T,Kunzelmann S,Herrmann Cdoi
10.1016/j.febslet.2009.05.027subject
Has Abstractpub_date
2009-06-18 00:00:00pages
1923-7issue
12eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00399-8journal_volume
583pub_type
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