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- W2011544361 abstract "Neuroglobin (Ngb) is a recently discovered vertebrate heme protein that is expressed in the brain and can reversibly bind oxygen. We previously demonstrated that ferric human Ngb binds to the α-subunits of heterotrimeric G proteins (Gα) and acts as a guanine nucleotide dissociation inhibitor (GDI) for Gα. Here we have investigated the interaction between Ngb and Gα in more detail. We report that zebrafish Ngb, which shares about 50% amino acid sequence identity with human Ngb, does not have a GDI activity for Gα. By carrying out exon swapping between zebrafish and human Ngb and site-directed mutagenesis, we have identified several residues that are crucial for the GDI activity of human Ngb." @default.
- W2011544361 created "2016-06-24" @default.
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- W2011544361 date "2005-02-05" @default.
- W2011544361 modified "2023-10-09" @default.
- W2011544361 title "Identification of Residues in Human Neuroglobin Crucial for Guanine Nucleotide Dissociation Inhibitor Activity" @default.
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- W2011544361 doi "https://doi.org/10.1021/bi0477539" @default.
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