Aug 1, 2000 · By mutating residues in the putative active site of yeast or animal Nit proteins, it may be possible to trap Nit substrates and use genetic approaches to discover the cellular …

Nit monomers possess a new alpha-beta-beta-alpha sandwich fold with a presumptive Cys-Glu-Lys catalytic triad. Nit assembles into a tetrameric, 52-stranded beta box that binds Fhit dimers …

Although substrates for Nit have not been identified, the crystal structure of worm NitFhit [10••] and the crystal structure of an N-carbamyl-d-amino acid amidohydrolase from Agrobacterium …

To determine the structure of Nit and the nature of Nit–Fhit interactions, worm NitFhit was crystallized and its crystal structure was determined. The 440 amino acid polypeptide …

Mar 17, 2000 · Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers. The nucleotide-binding protein Fhit, among the earliest and most …

Aug 1, 2000 · This study determined the crystal structure of Nit2 from Kluyveromyces lactis at 2.2 Å resolution and compared it with the structure of yeast-, worm-, and mouse-derived Nit2 …

Aug 1, 2000 · Nit assembles into a tetrameric, 52-stranded beta box that binds Fhit dimers at opposite poles and displays Nit active sites around the middle of the complex.

Dec 1, 2002 · A novel Glu-Lys-Cys catalytic triad, found at the crystallographically defined Nit active site of worm NitFhit, was postulated to constitute the catalytic residues for all members …

Aug 1, 2000 · To determine the structure of Nit and the nature of Nit–Fhit interactions, worm NitFhit was crystallized and its crystal structure was determined.

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