Structural characterization of human histidine triad nucleotide-binding protein 2, a member of the histidine triad superfamily
نویسندگان
چکیده
منابع مشابه
Structural characterization of human histidine triad nucleotide-binding protein 2, a member of the histidine triad superfamily.
The histidine triad proteins (HITs) constitute a large and ubiquitous superfamily of nucleotide hydrolases. The human histidine triad nucleotide-binding proteins (hHints) are a distinct class of HITs noted for their acyl-AMP hydrolase and phosphoramidase activity. The first high-resolution crystal structures of hHint2 with and without bound AMP are described. The differences between hHint2 and ...
متن کاملThe histidine triad superfamily of nucleotide-binding proteins.
Histidine triad (HIT) proteins were until recently a superfamily of proteins that shared only sequence motifs. Crystal structures of nucleotide-bound forms of histidine triad nucleotide-binding protein (Hint) demonstrated that the conserved residues in HIT proteins are responsible for their distinctive, dimeric, 10-stranded half-barrel structures that form two identical purine nucleotide-bindin...
متن کاملKinetic mechanism of human histidine triad nucleotide binding protein 1.
Human histidine triad nucleotide binding protein 1 (hHint1) is a member of a ubiquitous and ancient branch of the histidine triad protein superfamily. hHint1 is a homodimeric protein that catalyzes the hydrolysis of model substrates, phosphoramidate and acyl adenylate, with a high efficiency. Recently, catalytically inactive hHint1 has been identified as the cause of inherited peripheral neurop...
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It is currently thought that the transforming growth factor-β (TGF-β)/Smad signaling pathway acts as a central pathway leading to liver fibrosis, and that the aberrant Wnt/β-catenin signaling pathway also plays a vital role in the development of liver fibrosis. There is evidence that the histidine triad nucleotide-binding protein 1 (Hint1) was capable of inhibiting these two pathways. However, ...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2013
ISSN: 1742-464X
DOI: 10.1111/febs.12330